MyHits has reached its end of life and no longer provides data or services. Thank you for your support and trust for more than 23 years!
However, the webserver will remain online in its present form at least until end of March 2025.
To ensure the future of MyHits, we would be happy if a person or community would take over the resource or parts of it. Interested? Please contact us (myhits [at] sib.swiss).
Pagni M, Ioannidis V, Cerutti L, Zahn-Zabal M, Jongeneel CV, Hau J, Martin O, Kuznetsov D, Falquet L.
MyHits: improvements to an interactive resource for analyzing protein sequences.
Nucleic Acids Res. 2007 Jul; 35(Web Server issue):W433-7
However, the webserver will remain online in its present form at least until end of March 2025.
To ensure the future of MyHits, we would be happy if a person or community would take over the resource or parts of it. Interested? Please contact us (myhits [at] sib.swiss).
Pagni M, Ioannidis V, Cerutti L, Zahn-Zabal M, Jongeneel CV, Hau J, Martin O, Kuznetsov D, Falquet L.
MyHits: improvements to an interactive resource for analyzing protein sequences.
Nucleic Acids Res. 2007 Jul; 35(Web Server issue):W433-7
- MyHits
| Description | RecName: Full=Phosphoenolpyruvate-protein phosphotransferase {ECO:0000303|PubMed:1551842}; EC=2.7.3.9 {ECO:0000269|PubMed:1551842}; AltName: Full=Phosphotransferase system, enzyme I {ECO:0000303|PubMed:1551842}; |
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| MyHits synonyms | PT1_STACT , P23533 , B9DQ26 , EB31B4DB01D0611D |
 Legends: 1, ACT_SITE Tele-phosphohistidine intermediate. {ECO:0000250|UniProtKB:P08839, ECO:0000305|PubMed:16867985}; 2, ACT_SITE Proton donor. {ECO:0000250|UniProtKB:P08839, ECO:0000305|PubMed:16867985}; 3, Magnesium. {ECO:0000250|UniProtKB:P08839}; 4, BINDING Substrate. {ECO:0000269|PubMed:16867985}; 5, CONFLICT M -> I (in Ref. 1; AAA26664). {ECO:0000305}; 6, CONFLICT A -> AK (in Ref. 1; AAA26664). {ECO:0000305}; 7, CONFLICT R -> V (in Ref. 1; AAA26664). {ECO:0000305}; 8, REGION PEP binding. {ECO:0000269|PubMed:16867985}; 9, CONFLICT LLEEERANLKNEGYE -> FLKKNVLTLKMKAMK (in Ref. 1; AAA26664). {ECO:0000305}; 10, CONFLICT NPAILR -> ISNFSF (in Ref. 1; AAA26664). {ECO:0000305}; 11, ipfam:PEP-utilizers [T]; 12, ipat:PEP_ENZYMES_2 [T]; 13, ipfam:PEP-utilisers_N [T]; 14, ipat:PEP_ENZYMES_PHOS_SITE [T]; 15, STRAND {ECO:0000244|PDB:2HRO}; 16, HELIX {ECO:0000244|PDB:2HRO}; 17, TURN {ECO:0000244|PDB:2HRO}.
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ID PT1_STACT Reviewed; 573 AA.
AC P23533; B9DQ26;
DT 01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT 05-MAY-2009, sequence version 2.
DT 02-NOV-2016, entry version 113.
DE RecName: Full=Phosphoenolpyruvate-protein phosphotransferase {ECO:0000303|PubMed:1551842};
DE EC=2.7.3.9 {ECO:0000269|PubMed:1551842};
DE AltName: Full=Phosphotransferase system, enzyme I {ECO:0000303|PubMed:1551842};
GN Name=ptsI; OrderedLocusNames=Sca_0705;
OS Staphylococcus carnosus (strain TM300).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=396513;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, AND COFACTOR.
RX PubMed=1551842;
RA Kohlbrecher D., Eisermann R., Hengstenberg W.;
RT "Staphylococcal phosphoenolpyruvate-dependent phosphotransferase
RT system: molecular cloning and nucleotide sequence of the
RT Staphylococcus carnosus ptsI gene and expression and complementation
RT studies of the gene product.";
RL J. Bacteriol. 174:2208-2214(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TM300;
RX PubMed=19060169; DOI=10.1128/AEM.01982-08;
RA Rosenstein R., Nerz C., Biswas L., Resch A., Raddatz G.,
RA Schuster S.C., Goetz F.;
RT "Genome analysis of the meat starter culture bacterium Staphylococcus
RT carnosus TM300.";
RL Appl. Environ. Microbiol. 75:811-822(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-90.
RX PubMed=1901791; DOI=10.1111/j.1432-1033.1991.tb15875.x;
RA Eisermann R., Fischer R., Kessler U., Neubauer A., Hengstenberg W.;
RT "Staphylococcal phosphoenolpyruvate-dependent phosphotransferase
RT system. Purification and protein sequencing of the Staphylococcus
RT carnosus histidine-containing protein, and cloning and DNA sequencing
RT of the ptsH gene.";
RL Eur. J. Biochem. 197:9-14(1991).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) IN COMPLEX WITH SUBSTRATE
RP ANALOG, SUBUNIT, AND ACTIVE SITE.
RX PubMed=16867985; DOI=10.1074/jbc.M513721200;
RA Marquez J., Reinelt S., Koch B., Engelmann R., Hengstenberg W.,
RA Scheffzek K.;
RT "Structure of the full-length enzyme I of the phosphoenolpyruvate-
RT dependent sugar phosphotransferase system.";
RL J. Biol. Chem. 281:32508-32515(2006).
CC -!- FUNCTION: General (non sugar-specific) component of the
CC phosphoenolpyruvate-dependent sugar phosphotransferase system
CC (sugar PTS). This major carbohydrate active-transport system
CC catalyzes the phosphorylation of incoming sugar substrates
CC concomitantly with their translocation across the cell membrane.
CC Enzyme I transfers the phosphoryl group from phosphoenolpyruvate
CC (PEP) to the phosphoryl carrier protein (HPr).
CC {ECO:0000269|PubMed:1551842}.
CC -!- CATALYTIC ACTIVITY: Phosphoenolpyruvate + protein L-histidine =
CC pyruvate + protein N(pi)-phospho-L-histidine.
CC {ECO:0000269|PubMed:1551842}.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:P08839,
CC ECO:0000305|PubMed:1551842};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.44 uM for PEP {ECO:0000269|PubMed:1551842};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:16867985}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- DOMAIN: The N-terminal domain contains the HPr binding site, the
CC central domain the pyrophosphate/phosphate carrier histidine, and
CC the C-terminal domain the pyruvate binding site.
CC {ECO:0000250|UniProtKB:P08839}.
CC -!- MISCELLANEOUS: The reaction takes place in three steps, mediated
CC by a phosphocarrier histidine residue located on the surface of
CC the central domain. The two first partial reactions are catalyzed
CC at an active site located on the N-terminal domain, and the third
CC partial reaction is catalyzed at an active site located on the C-
CC terminal domain. For catalytic turnover, the central domain
CC swivels from the concave surface of the N-terminal domain to that
CC of the C-terminal domain. {ECO:0000250|UniProtKB:P08839}.
CC -!- SIMILARITY: Belongs to the PEP-utilizing enzyme family.
CC {ECO:0000305}.
DR EMBL; M69050; AAA26664.1; -; Genomic_DNA.
DR EMBL; AM295250; CAL27616.1; -; Genomic_DNA.
DR EMBL; X60766; CAA43176.1; -; Genomic_DNA.
DR PIR; B42374; B42374.
DR RefSeq; WP_015899959.1; NC_012121.1.
DR PDB; 2HRO; X-ray; 2.50 A; A=1-573.
DR PDBsum; 2HRO; -.
DR SMR; P23533; -.
DR STRING; 396513.Sca_0705; -.
DR KEGG; sca:SCA_0705; -.
DR PATRIC; 19602186; VBIStaCar105558_0708.
DR eggNOG; ENOG4105BZ3; Bacteria.
DR eggNOG; COG1080; LUCA.
DR HOGENOM; HOG000278513; -.
DR KO; K08483; -.
DR OMA; DYVLGFA; -.
DR BRENDA; 2.7.3.9; 5873.
DR EvolutionaryTrace; P23533; -.
DR Proteomes; UP000000444; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008965; F:phosphoenolpyruvate-protein phosphotransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0009401; P:phosphoenolpyruvate-dependent sugar phosphotransferase system; IEA:UniProtKB-KW.
DR Gene3D; 1.10.274.10; -; 1.
DR Gene3D; 3.20.20.60; -; 1.
DR Gene3D; 3.50.30.10; -; 1.
DR InterPro; IPR008279; PEP-util_enz_mobile_dom.
DR InterPro; IPR018274; PEP_util_AS.
DR InterPro; IPR000121; PEP_util_C.
DR InterPro; IPR023151; PEP_util_CS.
DR InterPro; IPR024692; PTS_EI.
DR InterPro; IPR006318; PTS_EI-like.
DR InterPro; IPR008731; PTS_EIN.
DR InterPro; IPR015813; Pyrv/PenolPyrv_Kinase-like_dom.
DR Pfam; PF05524; PEP-utilisers_N; 1.
DR Pfam; PF00391; PEP-utilizers; 1.
DR Pfam; PF02896; PEP-utilizers_C; 1.
DR PIRSF; PIRSF000732; PTS_enzyme_I; 1.
DR SUPFAM; SSF47831; SSF47831; 1.
DR SUPFAM; SSF51621; SSF51621; 1.
DR SUPFAM; SSF52009; SSF52009; 1.
DR TIGRFAMs; TIGR01417; PTS_I_fam; 1.
DR PROSITE; PS00742; PEP_ENZYMES_2; 1.
DR PROSITE; PS00370; PEP_ENZYMES_PHOS_SITE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Complete proteome; Cytoplasm; Kinase; Magnesium;
KW Metal-binding; Phosphotransferase system; Reference proteome;
KW Sugar transport; Transferase; Transport.
FT CHAIN 1 573 Phosphoenolpyruvate-protein
FT phosphotransferase.
FT /FTId=PRO_0000147087.
FT REGION 455 456 PEP binding.
FT {ECO:0000269|PubMed:16867985}.
FT ACT_SITE 190 190 Tele-phosphohistidine intermediate.
FT {ECO:0000250|UniProtKB:P08839,
FT ECO:0000305|PubMed:16867985}.
FT ACT_SITE 503 503 Proton donor.
FT {ECO:0000250|UniProtKB:P08839,
FT ECO:0000305|PubMed:16867985}.
FT METAL 432 432 Magnesium.
FT {ECO:0000250|UniProtKB:P08839}.
FT METAL 456 456 Magnesium.
FT {ECO:0000250|UniProtKB:P08839}.
FT BINDING 297 297 Substrate. {ECO:0000269|PubMed:16867985}.
FT BINDING 333 333 Substrate. {ECO:0000269|PubMed:16867985}.
FT BINDING 466 466 Substrate. {ECO:0000269|PubMed:16867985}.
FT CONFLICT 124 124 M -> I (in Ref. 1; AAA26664).
FT {ECO:0000305}.
FT CONFLICT 128 128 A -> AK (in Ref. 1; AAA26664).
FT {ECO:0000305}.
FT CONFLICT 406 420 LLEEERANLKNEGYE -> FLKKNVLTLKMKAMK (in
FT Ref. 1; AAA26664). {ECO:0000305}.
FT CONFLICT 479 484 NPAILR -> ISNFSF (in Ref. 1; AAA26664).
FT {ECO:0000305}.
FT CONFLICT 536 536 R -> V (in Ref. 1; AAA26664).
FT {ECO:0000305}.
FT STRAND 10 12 {ECO:0000244|PDB:2HRO}.
FT HELIX 37 66 {ECO:0000244|PDB:2HRO}.
FT STRAND 68 70 {ECO:0000244|PDB:2HRO}.
FT HELIX 73 81 {ECO:0000244|PDB:2HRO}.
FT HELIX 84 97 {ECO:0000244|PDB:2HRO}.
FT HELIX 101 117 {ECO:0000244|PDB:2HRO}.
FT HELIX 124 143 {ECO:0000244|PDB:2HRO}.
FT TURN 166 170 {ECO:0000244|PDB:2HRO}.
FT TURN 174 176 {ECO:0000244|PDB:2HRO}.
FT HELIX 190 197 {ECO:0000244|PDB:2HRO}.
FT HELIX 209 211 {ECO:0000244|PDB:2HRO}.
FT TURN 236 238 {ECO:0000244|PDB:2HRO}.
FT HELIX 239 244 {ECO:0000244|PDB:2HRO}.
FT HELIX 247 255 {ECO:0000244|PDB:2HRO}.
FT HELIX 256 258 {ECO:0000244|PDB:2HRO}.
FT STRAND 271 278 {ECO:0000244|PDB:2HRO}.
FT HELIX 279 281 {ECO:0000244|PDB:2HRO}.
FT HELIX 282 286 {ECO:0000244|PDB:2HRO}.
FT TURN 287 289 {ECO:0000244|PDB:2HRO}.
FT STRAND 291 297 {ECO:0000244|PDB:2HRO}.
FT HELIX 299 301 {ECO:0000244|PDB:2HRO}.
FT HELIX 311 324 {ECO:0000244|PDB:2HRO}.
FT TURN 325 327 {ECO:0000244|PDB:2HRO}.
FT STRAND 329 333 {ECO:0000244|PDB:2HRO}.
FT STRAND 344 346 {ECO:0000244|PDB:2HRO}.
FT HELIX 354 356 {ECO:0000244|PDB:2HRO}.
FT STRAND 357 359 {ECO:0000244|PDB:2HRO}.
FT HELIX 361 366 {ECO:0000244|PDB:2HRO}.
FT HELIX 368 381 {ECO:0000244|PDB:2HRO}.
FT HELIX 382 384 {ECO:0000244|PDB:2HRO}.
FT STRAND 385 393 {ECO:0000244|PDB:2HRO}.
FT HELIX 397 415 {ECO:0000244|PDB:2HRO}.
FT TURN 416 418 {ECO:0000244|PDB:2HRO}.
FT STRAND 426 431 {ECO:0000244|PDB:2HRO}.
FT HELIX 434 438 {ECO:0000244|PDB:2HRO}.
FT HELIX 440 446 {ECO:0000244|PDB:2HRO}.
FT STRAND 448 452 {ECO:0000244|PDB:2HRO}.
FT HELIX 454 462 {ECO:0000244|PDB:2HRO}.
FT HELIX 472 474 {ECO:0000244|PDB:2HRO}.
FT HELIX 480 495 {ECO:0000244|PDB:2HRO}.
FT STRAND 499 502 {ECO:0000244|PDB:2HRO}.
FT HELIX 505 508 {ECO:0000244|PDB:2HRO}.
FT TURN 510 512 {ECO:0000244|PDB:2HRO}.
FT HELIX 513 519 {ECO:0000244|PDB:2HRO}.
FT STRAND 522 526 {ECO:0000244|PDB:2HRO}.
FT HELIX 528 530 {ECO:0000244|PDB:2HRO}.
FT HELIX 531 539 {ECO:0000244|PDB:2HRO}.
FT HELIX 543 553 {ECO:0000244|PDB:2HRO}.
FT HELIX 559 569 {ECO:0000244|PDB:2HRO}.
CC --------------------------------------------------------------------------
CC The following FT lines are automated annotations from the MyHits database.
CC --------------------------------------------------------------------------
FT MYHIT 154 226 ipfam:PEP-utilizers [T]
FT MYHIT 448 466 ipat:PEP_ENZYMES_2 [T]
FT MYHIT 6 127 ipfam:PEP-utilisers_N [T]
FT MYHIT 185 196 ipat:PEP_ENZYMES_PHOS_SITE [T]
FT MYHIT 251 542 ipfam:PEP-utilizers_C [T]
SQ SEQUENCE 573 AA; 63299 MW; EB31B4DB01D0611D CRC64;
MAKQIKGIAA SDGVAIAKAY LLVEPDLSFD NESVTDTDAE VAKFNGALNK SKVELTKIRN
NAEKQLGADK AAIFDAHLLV LEDPELIQPI EDKIKNESVN AAQALTDVSN QFITIFESMD
NEYMAERAAD IRDVSKRVLA HILGVELPNP SIVDESVVII GNDLTPSDTA QLNKEYVQGF
VTNIGGRTSH SAIMSRSLEI PAVVGTKSIT EEVEAGDTIV VDGMTGDVLI NPSDEVIAEY
QEKRENFFKD KQELQKLRDA ESVTADGHHV ELAANIGTPN DLPGVIENGA EGIGLYRTEF
LYMGRDQMPT EEEQFEAYKA VLEAMKGKRV VVRTLDIGGD KELPYLDLPE EMNPFLGYRA
IRLCLDQPEI FRPQLRALLR ASVFGKLNIM FPMVATIQEF RDAKALLEEE RANLKNEGYE
VADDIELGIM VEIPSTAALA DIFAKEVDFF SIGTNDLIQY TMAADRMSER VSYLYQPYNP
AILRLVKQVI EASHAEGKWT GMCGEMAGDQ TAIPLLLGLG LDEFSMSATS ILKARRLIRS
LNESEMKELS ERAVQCATSE EVVDLVEEYT KNA
//
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