ID SECA_LACPL Reviewed; 787 AA. AC Q88YL7; F9ULW7; DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-2003, sequence version 1. DT 22-JUL-2015, entry version 84. DE RecName: Full=Protein translocase subunit SecA {ECO:0000255|HAMAP-Rule:MF_01382}; GN Name=secA {ECO:0000255|HAMAP-Rule:MF_01382}; GN OrderedLocusNames=lp_0739; OS Lactobacillus plantarum (strain ATCC BAA-793 / NCIMB 8826 / WCFS1). OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae; OC Lactobacillus. OX NCBI_TaxID=220668; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-793 / NCIMB 8826 / WCFS1; RX PubMed=12566566; DOI=10.1073/pnas.0337704100; RA Kleerebezem M., Boekhorst J., van Kranenburg R., Molenaar D., RA Kuipers O.P., Leer R., Tarchini R., Peters S.A., Sandbrink H.M., RA Fiers M.W.E.J., Stiekema W., Klein Lankhorst R.M., Bron P.A., RA Hoffer S.M., Nierop Groot M.N., Kerkhoven R., De Vries M., Ursing B., RA De Vos W.M., Siezen R.J.; RT "Complete genome sequence of Lactobacillus plantarum WCFS1."; RL Proc. Natl. Acad. Sci. U.S.A. 100:1990-1995(2003). 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 as an ATP-driven molecular CC motor driving the stepwise translocation of polypeptide chains CC across the membrane. {ECO:0000255|HAMAP-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. Other proteins may also be involved. CC {ECO:0000255|HAMAP-Rule:MF_01382}. CC -!- SUBCELLULAR LOCATION: Cell 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AL935263; CCC78206.1; -; Genomic_DNA. DR RefSeq; WP_003643952.1; NC_004567.2. DR RefSeq; YP_004888720.1; NC_004567.2. DR ProteinModelPortal; Q88YL7; -. DR SMR; Q88YL7; 12-781. DR STRING; 220668.lp_0739; -. DR EnsemblBacteria; CCC78206; CCC78206; lp_0739. DR GeneID; 1063458; -. DR KEGG; lpl:lp_0739; -. DR PATRIC; 22247899; VBILacPla27411_0622. DR eggNOG; COG0653; -. DR HOGENOM; HOG000218169; -. DR KO; K03070; -. DR OMA; IATERHE; -. DR BioCyc; LPLA220668-WGS:GSPK-641-MONOMER; -. DR Proteomes; UP000000432; Chromosome. 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: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; 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; 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; 1. 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 membrane; Complete proteome; Cytoplasm; Membrane; KW Nucleotide-binding; Protein transport; Reference proteome; KW Translocation; Transport. FT CHAIN 1 787 Protein translocase subunit SecA. FT /FTId=PRO_1000073483. FT NP_BIND 100 107 ATP. {ECO:0000255|HAMAP-Rule:MF_01382}. SQ SEQUENCE 787 AA; 89558 MW; D97CE603A4294E50 CRC64; MANILKRWVE SDKRTIRRLD KIANKVEAYA DEYGKLSDAD LQAKTPEFRE RYKEGESLDD LLPEAFATAR EGAKRVLGLY PFHVQILGGI VLHQGDIAEM KTGEGKTLTA TMPVYLNAIS GKGVHVVTVN EYLSARDATE MGELYNWLGM SVGINGAEKS PEEKRAAYNA DITYSTNGEI GFDYLRDNMV VYREDMVQRP LNFAIIDEVD SILIDEARTP LIISGQSEGT TGMYKRADRF AKTLTKDEDY KVDLESKTVA LLDEGIRKAE KYFGLENLYD TDNTALNHYL DEALRANYIM LKDKDYVISD GQALIVDSFT GRIMDGRRFS DGLHQAIEAK EHVEIQEETK TMANITYQNL FRMYKKLSGM TGTAKTEQEE FREIYNMEVI TIPTNRPMIR DDRSDLLYPT LQSKFNAVVK EIKQLHEKGQ PMLIGTVAVE TSEYLSHRLD EENIPHVVLN AKNHAKEADI VANAGQRGAV TIATNMAGRG TDIKLGPGVK EVGGLAVIGT ERHESRRIDN QLRGRAGRQG DPGMSQFYLS LEDDLMLRFG SERIKNFLQR MNVEDDDAVI QSRMITRQVE SAQKRVEGNN YDSRKNVLQY DDVMRAQREV IYGERQQVIM EEKSLKPVIM PMIKRTVERT VQLHMQGDAK DWDLDAVVDF AQAAMVKEDS ISVADLKGKS PAEVEAYLMD RVDKIYADKA KQLYDAGQML EFEKVVILRV VDSHWTDHID AMDQLRQSIG LRGYGQLNPL VEYQRDGYQM FEEMVADIDY DTTRLFMKSE IRQNIQR //