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 03-MAY-2023, entry version 119. DE RecName: Full=Protein translocase subunit SecA {ECO:0000255|HAMAP-Rule:MF_01382}; DE EC=7.4.2.8 {ECO:0000255|HAMAP-Rule:MF_01382}; GN Name=secA {ECO:0000255|HAMAP-Rule:MF_01382}; OrderedLocusNames=lp_0739; OS Lactiplantibacillus plantarum (strain ATCC BAA-793 / NCIMB 8826 / WCFS1) OS (Lactobacillus plantarum). OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae; OC Lactiplantibacillus. 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., Kuipers O.P., RA Leer R., Tarchini R., Peters S.A., Sandbrink H.M., Fiers M.W.E.J., RA Stiekema W., Klein Lankhorst R.M., Bron P.A., Hoffer S.M., RA Nierop Groot M.N., Kerkhoven R., De Vries M., Ursing B., De Vos W.M., RA Siezen R.J.; RT "Complete genome sequence of Lactobacillus plantarum WCFS1."; RL Proc. Natl. Acad. Sci. U.S.A. 100:1990-1995(2003). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION. RC STRAIN=ATCC BAA-793 / NCIMB 8826 / WCFS1; RX PubMed=22156394; DOI=10.1128/jb.06275-11; RA Siezen R.J., Francke C., Renckens B., Boekhorst J., Wels M., RA Kleerebezem M., van Hijum S.A.; RT "Complete resequencing and reannotation of the Lactobacillus plantarum RT WCFS1 genome."; RL J. Bacteriol. 194:195-196(2012). CC -!- FUNCTION: Part of the Sec protein translocase complex. Interacts with CC the SecYEG preprotein conducting channel. Has a central role in CC coupling the hydrolysis of ATP to the transfer of proteins into and CC across the cell membrane, serving as an ATP-driven molecular motor CC driving the stepwise translocation of polypeptide chains across the CC membrane. {ECO:0000255|HAMAP-Rule:MF_01382}. CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + H2O + cellular proteinSide 1 = ADP + phosphate + CC cellular proteinSide 2.; EC=7.4.2.8; Evidence={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. Other proteins may also be involved. CC {ECO:0000255|HAMAP-Rule:MF_01382}. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|HAMAP-Rule:MF_01382}; CC Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_01382}; CC Cytoplasmic side {ECO:0000255|HAMAP-Rule:MF_01382}. Cytoplasm CC {ECO:0000255|HAMAP-Rule:MF_01382}. Note=Distribution is 50-50. CC {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 AlphaFoldDB; Q88YL7; -. DR SMR; Q88YL7; -. DR STRING; 220668.lp_0739; -. DR EnsemblBacteria; CCC78206; CCC78206; lp_0739. DR KEGG; lpl:lp_0739; -. DR PATRIC; fig|220668.9.peg.622; -. DR eggNOG; COG0653; Bacteria. DR HOGENOM; CLU_005314_3_2_9; -. DR OMA; MVHYDVQ; -. DR OrthoDB; 9805579at2; -. DR PhylomeDB; Q88YL7; -. DR BioCyc; LPLA220668:G1GW0-641-MON; -. 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-UniRule. DR GO; GO:0008564; F:protein-exporting ATPase activity; IEA:UniProtKB-EC. DR GO; GO:0065002; P:intracellular protein transmembrane transport; IEA:UniProtKB-UniRule. DR GO; GO:0017038; P:protein import; IEA:InterPro. DR GO; GO:0006605; P:protein targeting; IEA:UniProtKB-UniRule. DR CDD; cd17928; DEXDc_SecA; 1. DR CDD; cd18803; SF2_C_secA; 1. DR Gene3D; 1.10.3060.10; Helical scaffold and wing domains of SecA; 1. DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2. DR Gene3D; 3.90.1440.10; SecA, preprotein cross-linking domain; 1. DR HAMAP; MF_01382; SecA; 1. DR InterPro; IPR014001; Helicase_ATP-bd. DR InterPro; IPR001650; Helicase_C. 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; IPR044722; SecA_SF2_C. DR InterPro; IPR011116; SecA_Wing/Scaffold. DR InterPro; IPR036266; SecA_Wing/Scaffold_sf. DR InterPro; IPR036670; SecA_X-link_sf. DR PANTHER; PTHR30612; SECA INNER MEMBRANE COMPONENT OF SEC PROTEIN SECRETION SYSTEM; 1. DR PANTHER; PTHR30612:SF0; SI:DKEY-187J14.7-RELATED; 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; SSF81886; Helical scaffold and wing domains of SecA; 1. DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2. DR SUPFAM; SSF81767; Pre-protein crosslinking domain of SecA; 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; Cytoplasm; Membrane; Nucleotide-binding; KW Protein transport; Reference proteome; Translocase; Translocation; KW Transport. FT CHAIN 1..787 FT /note="Protein translocase subunit SecA" FT /id="PRO_1000073483" FT BINDING 85 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01382" FT BINDING 103..107 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01382" FT BINDING 492 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="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 //