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=Alpha-hemolysin translocation ATP-binding protein HlyB; |
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| MyHits synonyms | HLYBC_ECOLX , P10089 , 21009CB45E59437E |
 Legends: 1, ACT_SITE {ECO:0000255|PROSITE-ProRule:PRU00362}; 2, TRANSMEM Helical. {ECO:0000255|PROSITE- ProRule:PRU00441}; 3, Peptidase C39. {ECO:0000255|PROSITE- ProRule:PRU00362}; 4, ABC transmembrane type-1. {ECO:0000255|PROSITE-ProRule:PRU00441}; 5, ABC transporter. {ECO:0000255|PROSITE- ProRule:PRU00362, ECO:0000255|PROSITE- ProRule:PRU00434}; 6, NP_BIND ATP. {ECO:0000255|PROSITE- ProRule:PRU00362, ECO:0000255|PROSITE- ProRule:PRU00434}; 7, ipfam:Peptidase_C39 [T]; 8, iprf:PEPTIDASE_C39 [T]; 9, ipat:ABC_TRANSPORTER_1 [T].
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ID HLYBC_ECOLX Reviewed; 707 AA.
AC P10089;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 2.
DT 02-NOV-2016, entry version 116.
DE RecName: Full=Alpha-hemolysin translocation ATP-binding protein HlyB;
GN Name=hlyB;
OS Escherichia coli.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=562;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=J96 / Serotype O4;
RX PubMed=3891743;
RA Felmlee T., Pellett S., Welch R.A.;
RT "Nucleotide sequence of an Escherichia coli chromosomal hemolysin.";
RL J. Bacteriol. 163:94-105(1985).
CC -!- FUNCTION: Part of the ABC transporter complex HlyBD involved in
CC hemolysin export. Transmembrane domains (TMD) form a pore in the
CC inner membrane and the ATP-binding domain (NBD) is responsible for
CC energy generation (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Homodimer.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000305}; Multi-
CC pass membrane protein {ECO:0000305}.
CC -!- DOMAIN: In HlyB the peptidase C39 domain, the ATP-binding domain
CC (NBD) and the transmembrane domain (TMD) are fused.
CC -!- MISCELLANEOUS: The complex HlyBD-TolC (OMF) forms a single
CC transport channel across the two membranes, allowing direct export
CC of alpha-hemolysin. These channel is involved in type 1 secretion
CC system (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. Protein-1
CC exporter (TC 3.A.1.109) family. {ECO:0000305}.
CC -!- SIMILARITY: Contains 1 ABC transmembrane type-1 domain.
CC {ECO:0000255|PROSITE-ProRule:PRU00441}.
CC -!- SIMILARITY: Contains 1 ABC transporter domain.
CC {ECO:0000255|PROSITE-ProRule:PRU00362, ECO:0000255|PROSITE-
CC ProRule:PRU00434}.
CC -!- SIMILARITY: Contains 1 peptidase C39 domain. {ECO:0000255|PROSITE-
CC ProRule:PRU00362}.
CC -!- CAUTION: Tyr-9 is present instead of the conserved Cys which is
CC expected to be the active site residue of peptidase C39. Thus they
CC are presumed to be without peptidase activity. {ECO:0000305}.
DR EMBL; M10133; AAA23976.1; -; Genomic_DNA.
DR RefSeq; WP_021525012.1; NZ_JSGE01000112.1.
DR ProteinModelPortal; P10089; -.
DR DIP; DIP-16931N; -.
DR STRING; 199310.c3573; -.
DR eggNOG; ENOG4108JJA; Bacteria.
DR eggNOG; COG2274; LUCA.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0030256; C:type I protein secretion system complex; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0042626; F:ATPase activity, coupled to transmembrane movement of substances; IEA:InterPro.
DR GO; GO:0008233; F:peptidase activity; IEA:InterPro.
DR GO; GO:0008565; F:protein transporter activity; IEA:InterPro.
DR GO; GO:0030253; P:protein secretion by the type I secretion system; IEA:InterPro.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR011527; ABC1_TM_dom.
DR InterPro; IPR003439; ABC_transporter-like.
DR InterPro; IPR017871; ABC_transporter_CS.
DR InterPro; IPR010132; ATPase_T1SS_HlyB.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR005074; Peptidase_C39.
DR Pfam; PF00664; ABC_membrane; 1.
DR Pfam; PF00005; ABC_tran; 1.
DR Pfam; PF03412; Peptidase_C39; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF90123; SSF90123; 1.
DR TIGRFAMs; TIGR01846; type_I_sec_HlyB; 1.
DR PROSITE; PS50929; ABC_TM1F; 1.
DR PROSITE; PS00211; ABC_TRANSPORTER_1; 1.
DR PROSITE; PS50893; ABC_TRANSPORTER_2; 1.
DR PROSITE; PS50990; PEPTIDASE_C39; 1.
PE 3: Inferred from homology;
KW ATP-binding; Cell inner membrane; Cell membrane; Hydrolase; Membrane;
KW Nucleotide-binding; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1 707 Alpha-hemolysin translocation ATP-binding
FT protein HlyB.
FT /FTId=PRO_0000092372.
FT TRANSMEM 158 178 Helical. {ECO:0000255|PROSITE-
FT ProRule:PRU00441}.
FT TRANSMEM 191 211 Helical. {ECO:0000255|PROSITE-
FT ProRule:PRU00441}.
FT TRANSMEM 269 289 Helical. {ECO:0000255|PROSITE-
FT ProRule:PRU00441}.
FT TRANSMEM 295 315 Helical. {ECO:0000255|PROSITE-
FT ProRule:PRU00441}.
FT TRANSMEM 388 408 Helical. {ECO:0000255|PROSITE-
FT ProRule:PRU00441}.
FT DOMAIN 3 125 Peptidase C39. {ECO:0000255|PROSITE-
FT ProRule:PRU00362}.
FT DOMAIN 154 436 ABC transmembrane type-1.
FT {ECO:0000255|PROSITE-ProRule:PRU00441}.
FT DOMAIN 468 703 ABC transporter. {ECO:0000255|PROSITE-
FT ProRule:PRU00362, ECO:0000255|PROSITE-
FT ProRule:PRU00434}.
FT NP_BIND 502 509 ATP. {ECO:0000255|PROSITE-
FT ProRule:PRU00362, ECO:0000255|PROSITE-
FT ProRule:PRU00434}.
FT ACT_SITE 83 83 {ECO:0000255|PROSITE-ProRule:PRU00362}.
CC --------------------------------------------------------------------------
CC The following FT lines are automated annotations from the MyHits database.
CC --------------------------------------------------------------------------
FT MYHIT 8 129 ipfam:Peptidase_C39 [T]
FT MYHIT 157 424 ipfam:ABC_membrane [T]
FT MYHIT 468 703 iprf:ABC_TRANSPORTER_2 [T]
FT MYHIT 3 125 iprf:PEPTIDASE_C39 [T]
FT MYHIT 494 680 ismart:AAA [T]
FT MYHIT 485 634 ipfam:ABC_tran [T]
FT MYHIT 158 436 iprf:ABC_TM1F [T]
FT MYHIT 606 620 ipat:ABC_TRANSPORTER_1 [T]
SQ SEQUENCE 707 AA; 79464 MW; 21009CB45E59437E CRC64;
MDSCHKIDYG LYALEILAQY HNVSVNPEEI KHRFDTDGTG LGLTSWLLAA KSLELKVKQV
KKTIDRLNFI SLPALVWRED GCHFILTKVS KEANRYLIFD LEQRNPRVLE QSEFEALYQG
HIILIASRSS VTGKLAKFDF TWFIPAIIKY RKIFIETLVV SVFLQLFALI TPLFFQVVMD
KVLVHRGFST LNVITVALSV VVVFEIILSG LRTYIFAHST SRIDVELGAK LFRHLLALPI
SYFESRRVGD TVARVRELDQ IRNFLTGQAL TSVLDLLFSF IFFAVMWYYS PKLTLVILFS
LPCYAAWSVF ISPILRRRLD DKFSRNADNQ SFLVESVTAI NTIKAMAVSP QMTNIWDKQL
AGYVAAGFKV TVLATIGQQG IQLIQKTVMI INLWLGAHLV ISGDLSIGQL IAFNMLAGQI
VAPVIRLAQI WQDFQQVGIS VTRLGDVLNS PTESYHGKLA LPEINGDITF RNIRFRYKPD
SPVILDNINL SIKQGEVIGI VGRSGSGKST LTKLIQRFYI PENGQVLIDG HDLALADPNW
LRRQVGVVLQ DNVLLNRSII DNISLANPGM SVEKVIYAAK LAGAHDFISE LREGYNTIVG
EQGAGLSGGQ RQRIAIARAL VNNPKILIFD EATSALDYES EHVIMRNMHK ICKGRTVIII
AHRLSTVKNA DRIIVMEKGK IVEQGKHKEL LSEPESLYSY LYQLQSD
//
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