ID SECA_BURXL Reviewed; 936 AA.
AC Q13U01;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 22-AUG-2006, sequence version 1.
DT 02-NOV-2016, entry version 79.
DE RecName: Full=Protein translocase subunit SecA {ECO:0000255|HAMAP-Rule:MF_01382};
GN Name=secA {ECO:0000255|HAMAP-Rule:MF_01382};
GN OrderedLocusNames=Bxeno_A3900; ORFNames=Bxe_A0495;
OS Burkholderia xenovorans (strain LB400).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Paraburkholderia.
OX NCBI_TaxID=266265;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LB400;
RX PubMed=17030797; DOI=10.1073/pnas.0606924103;
RA Chain P.S.G., Denef V.J., Konstantinidis K.T., Vergez L.M., Agullo L.,
RA Reyes V.L., Hauser L., Cordova M., Gomez L., Gonzalez M., Land M.,
RA Lao V., Larimer F., LiPuma J.J., Mahenthiralingam E., Malfatti S.A.,
RA Marx C.J., Parnell J.J., Ramette A., Richardson P., Seeger M.,
RA Smith D., Spilker T., Sul W.J., Tsoi T.V., Ulrich L.E., Zhulin I.B.,
RA Tiedje J.M.;
RT "Burkholderia xenovorans LB400 harbors a multi-replicon, 9.73-Mbp
RT genome shaped for versatility.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:15280-15287(2006).
CC -!- FUNCTION: Part of the Sec protein translocase complex. Interacts
CC with the SecYEG preprotein conducting channel. Has a central role
CC in coupling the hydrolysis of ATP to the transfer of proteins into
CC and across the cell membrane, serving both as a receptor for the
CC preprotein-SecB complex and as an ATP-driven molecular motor
CC driving the stepwise translocation of polypeptide chains across
CC the membrane. {ECO:0000255|HAMAP-Rule:MF_01382}.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01382};
CC Note=May bind 1 zinc ion per subunit. {ECO:0000255|HAMAP-
CC Rule:MF_01382};
CC -!- SUBUNIT: Monomer and homodimer. Part of the essential Sec protein
CC translocation apparatus which comprises SecA, SecYEG and auxiliary
CC proteins SecDF-YajC and YidC. {ECO:0000255|HAMAP-Rule:MF_01382}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC Rule:MF_01382}; Peripheral membrane protein {ECO:0000255|HAMAP-
CC Rule:MF_01382}; Cytoplasmic side {ECO:0000255|HAMAP-
CC Rule:MF_01382}. Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01382}.
CC Note=Distribution is 50-50. {ECO:0000255|HAMAP-Rule:MF_01382}.
CC -!- SIMILARITY: Belongs to the SecA family. {ECO:0000255|HAMAP-
CC Rule:MF_01382}.
DR EMBL; CP000270; ABE32438.1; -; Genomic_DNA.
DR RefSeq; WP_011489910.1; NZ_CP008760.1.
DR ProteinModelPortal; Q13U01; -.
DR STRING; 266265.Bxe_A0495; -.
DR PRIDE; Q13U01; -.
DR EnsemblBacteria; ABE32438; ABE32438; Bxe_A0495.
DR GeneID; 4005917; -.
DR KEGG; bxb:DR64_2671; -.
DR KEGG; bxe:Bxe_A0495; -.
DR PATRIC; 19333657; VBIBurXen52548_4121.
DR eggNOG; ENOG4105CI6; Bacteria.
DR eggNOG; COG0653; LUCA.
DR HOGENOM; HOG000218168; -.
DR KO; K03070; -.
DR OMA; IATERHE; -.
DR OrthoDB; POG091H01RS; -.
DR Proteomes; UP000001817; Chromosome 1.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0065002; P:intracellular protein transmembrane transport; IEA:UniProtKB-HAMAP.
DR GO; GO:0017038; P:protein import; IEA:InterPro.
DR GO; GO:0006605; P:protein targeting; IEA:UniProtKB-HAMAP.
DR Gene3D; 1.10.3060.10; -; 1.
DR Gene3D; 3.40.50.300; -; 3.
DR Gene3D; 3.90.1440.10; -; 1.
DR HAMAP; MF_01382; SecA; 1.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR004027; SEC_C_motif.
DR InterPro; IPR000185; SecA.
DR InterPro; IPR020937; SecA_CS.
DR InterPro; IPR011115; SecA_DEAD.
DR InterPro; IPR014018; SecA_motor_DEAD.
DR InterPro; IPR011130; SecA_preprotein_X-link_dom.
DR InterPro; IPR011116; SecA_Wing/Scaffold.
DR Pfam; PF02810; SEC-C; 1.
DR Pfam; PF07517; SecA_DEAD; 1.
DR Pfam; PF01043; SecA_PP_bind; 1.
DR Pfam; PF07516; SecA_SW; 1.
DR PRINTS; PR00906; SECA.
DR SMART; SM00957; SecA_DEAD; 1.
DR SMART; SM00958; SecA_PP_bind; 1.
DR SUPFAM; SSF52540; SSF52540; 3.
DR SUPFAM; SSF81767; SSF81767; 1.
DR SUPFAM; SSF81886; SSF81886; 2.
DR TIGRFAMs; TIGR00963; secA; 1.
DR PROSITE; PS01312; SECA; 1.
DR PROSITE; PS51196; SECA_MOTOR_DEAD; 1.
PE 3: Inferred from homology;
KW ATP-binding; Cell inner membrane; Cell membrane; Complete proteome;
KW Cytoplasm; Membrane; Metal-binding; Nucleotide-binding;
KW Protein transport; Reference proteome; Translocation; Transport; Zinc.
FT CHAIN 1 936 Protein translocase subunit SecA.
FT /FTId=PRO_0000320759.
FT NP_BIND 102 109 ATP. {ECO:0000255|HAMAP-Rule:MF_01382}.
FT METAL 920 920 Zinc. {ECO:0000255|HAMAP-Rule:MF_01382}.
FT METAL 922 922 Zinc. {ECO:0000255|HAMAP-Rule:MF_01382}.
FT METAL 931 931 Zinc. {ECO:0000255|HAMAP-Rule:MF_01382}.
FT METAL 932 932 Zinc. {ECO:0000255|HAMAP-Rule:MF_01382}.
CC --------------------------------------------------------------------------
CC The following FT lines are automated annotations from the MyHits database.
CC --------------------------------------------------------------------------
FT MYHIT 916 934 ipfam:SEC-C [T]
FT MYHIT 233 361 ipfam:SecA_PP_bind [T]
FT MYHIT 503 518 ipat:SECA [T]
FT MYHIT 228 361 ismart:SecA_PP_bind [T]
FT MYHIT 5 842 ihamap:SecA [T]
FT MYHIT 6 405 ipfam:SecA_DEAD [T]
FT MYHIT 3 629 iprf:SECA_MOTOR_DEAD [T]
FT MYHIT 6 405 ismart:SecA_DEAD [T]
FT MYHIT 627 840 ipfam:SecA_SW [T]
SQ SEQUENCE 936 AA; 105120 MW; 9379E8DD955B6869 CRC64;
MTTGFLQKIF GSRNQRLVKQ YQKTVAAINA LEPQIEQLTD DQLRGKTGEF RQRVASGESL
DKLLPEAFAV CREASKRVLK MRHFDVQLIG GMVLHYGKIG EMRTGEGKTL VATLPVYLNA
LSGRGVHVVT VNDYLAQRDA EWMARLYNFL GLSVGINLSQ MDHAAKQEAY AADITYGTNN
EFGFDYLRDN MVYETDARVQ RALNFAVVDE VDSILIDEAR TPLIISGQAE DHTELYVRMN
ALPPLLERQI GEEKADGTGV EKPGDYTLDE KGRQVFLTES GHEKAERLLS EWGLIGEGES
LYAPQNITLM HHVYAALRAH TLFFKDQHYV VQNGEVVIVD EFTGRLMSGR RWSDGLHQAV
EAKEHVKIQS ENQTLASITF QNYFRMYAKL SGMTGTADTE AYEFNEIYGL ETVVIPTNRP
PKRIDKQDQI YKTAKERYDA VIRDIRDCYE RGQPVLVGTT SIENSELLSH LLKQAGLPHE
VLNAKQHARE AEIVAEAGRP KRITIATNMA GRGTDIVLGG NAEKQASFLE LDETLPEDEK
RRRIQKLHDE WQALHDQVKA AGGLHIIGTE RHESRRIDNQ LRGRAGRQGD PGSSRFYLSL
EDPLLRIFAG DRVRAIMERL KMPEGEAIEA GIVSRSIESA QRKVEARNFD IRKQLLEYDD
VSNDQRKVIY QQRNELLEAN DITETIGAMR QSVIADIVHQ FVPAGSIEEQ WDVPELEEVL
RNEWQLDLAI QEMINESNSI SADEILEAVE AAADEAYEAK VELVGRESFS AFERSIMLQT
LDRSWREHLA ALDHLRQGIH LRGYAQKNPK QEYKREAFEL FAAMLDAVKL EVTRVVMNVQ
IQSPEQLEQA AEQLEEQGSH LENVEFRHAE FAEAAAAAPV AAEAATAAMI GDAMSHGSSQ
AAAANMSADN VPKVGRNDPC PCGSGKKYKQ CHGKIV
//
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