ID W7D426_9LIST Unreviewed; 827 AA. AC W7D426; DT 16-APR-2014, integrated into UniProtKB/TrEMBL. DT 16-APR-2014, sequence version 1. DT 24-JAN-2024, entry version 37. DE RecName: Full=Protein translocase subunit SecA {ECO:0000256|HAMAP-Rule:MF_01382, ECO:0000256|RuleBase:RU003874}; DE EC=7.4.2.8 {ECO:0000256|HAMAP-Rule:MF_01382}; GN Name=secA {ECO:0000256|HAMAP-Rule:MF_01382}; GN ORFNames=BCAMP_06295 {ECO:0000313|EMBL:EUJ40033.1}; OS Brochothrix campestris FSL F6-1037. OC Bacteria; Bacillota; Bacilli; Bacillales; Listeriaceae; Brochothrix. OX NCBI_TaxID=1265861 {ECO:0000313|EMBL:EUJ40033.1, ECO:0000313|Proteomes:UP000019243}; RN [1] {ECO:0000313|EMBL:EUJ40033.1, ECO:0000313|Proteomes:UP000019243} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=FSL F6-1037 {ECO:0000313|EMBL:EUJ40033.1, RC ECO:0000313|Proteomes:UP000019243}; RA den Bakker H.C., Allred A., Warchocki S., Wright E.M., Burrell A., RA Nightingale K.K., Kephart D., Wiedmann M.; RT "Novel taxa of Listeriaceae from agricultural environments in the United RT States."; RL Submitted (DEC-2012) to the EMBL/GenBank/DDBJ databases. 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:0000256|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:0000256|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:0000256|HAMAP-Rule:MF_01382}. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|HAMAP-Rule:MF_01382}; CC Peripheral membrane protein {ECO:0000256|HAMAP-Rule:MF_01382}; CC Cytoplasmic side {ECO:0000256|HAMAP-Rule:MF_01382}. Cytoplasm CC {ECO:0000256|HAMAP-Rule:MF_01382}. Note=Distribution is 50-50. CC {ECO:0000256|HAMAP-Rule:MF_01382}. CC -!- SIMILARITY: Belongs to the SecA family. {ECO:0000256|ARBA:ARBA00007650, CC ECO:0000256|HAMAP-Rule:MF_01382, ECO:0000256|RuleBase:RU003874}. CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ CC whole genome shotgun (WGS) entry which is preliminary data. CC {ECO:0000313|EMBL:EUJ40033.1}. 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; AODH01000022; EUJ40033.1; -; Genomic_DNA. DR AlphaFoldDB; W7D426; -. DR STRING; 1265861.BCAMP_06295; -. DR PATRIC; fig|1265861.3.peg.1246; -. DR Proteomes; UP000019243; Unassembled WGS sequence. 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: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 NCBIfam; TIGR00963; secA; 1. 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; PF21090; P-loop_SecA; 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 PROSITE; PS51192; HELICASE_ATP_BIND_1; 1. DR PROSITE; PS51194; HELICASE_CTER; 1. DR PROSITE; PS01312; SECA; 1. DR PROSITE; PS51196; SECA_MOTOR_DEAD; 1. PE 3: Inferred from homology; KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP- KW Rule:MF_01382}; KW Cell membrane {ECO:0000256|ARBA:ARBA00022475, ECO:0000256|HAMAP- KW Rule:MF_01382}; KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_01382}; KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_01382}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP- KW Rule:MF_01382}; KW Protein transport {ECO:0000256|ARBA:ARBA00022927, ECO:0000256|HAMAP- KW Rule:MF_01382}; Reference proteome {ECO:0000313|Proteomes:UP000019243}; KW Translocase {ECO:0000256|ARBA:ARBA00022967, ECO:0000256|HAMAP- KW Rule:MF_01382}; KW Translocation {ECO:0000256|ARBA:ARBA00023010, ECO:0000256|HAMAP- KW Rule:MF_01382}; KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|HAMAP-Rule:MF_01382}. FT DOMAIN 1..569 FT /note="SecA family profile" FT /evidence="ECO:0000259|PROSITE:PS51196" FT DOMAIN 87..245 FT /note="Helicase ATP-binding" FT /evidence="ECO:0000259|PROSITE:PS51192" FT DOMAIN 409..584 FT /note="Helicase C-terminal" FT /evidence="ECO:0000259|PROSITE:PS51194" FT REGION 787..827 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 85 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01382" FT BINDING 103..107 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01382" FT BINDING 491 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01382" SQ SEQUENCE 827 AA; 93388 MW; D9DC6E61376FF6CC CRC64; MAGLLKKLFE SGKKDEKYLE KKVALVEARA DEMAVLTDEQ LKQKTIEFKE RVQQGETLDQ LLPEAFAVAR EGAKRVLGMY PFPVQIMGGI VLHEGNVAEM KTGEGKTLTS TLPVYLNALS GKGVHVVTVN EYLVQRDALE MGQLYEFLGL TVGININALS TDEKREKYAC DITYSTNNEL GFDYLRDNMV VYKEQMVQRP LSFAVIDEVD SILIDEARTP LIISGEAEKS TLGYNRASTF VKTLTEDSYI YDLKTKAVSL NEDGMDKAEK FFQVDNIFDL ANASILHYIA QALKAEVTMH KDVDYVVQDD EVLIVDQFTG RIMEGRRFSD GLHQSIEAKE GVAIKSESKT MATITFQNYF RMYEKLSGMT GTAKTEEEEL TDIYNMRVIQ IPTNKPIQRE DHADLIYGSI AAKFEAVAED IAARHLKGQP VLVGTVAIET SELISEKLTR KGIPHNVLNA KQHEREADII TNAGLKGAVT IATNMAGRGT DIKLGEGVIE AGGLAVIGTE RHESRRIDNQ LRGRAGRQGD PGATQFYLSM EDELMKRFSS DNVKRMMDRF MGENEAIQSK MLSRAVESAQ TRVEGNNFDS RKQVLQYDDV LRQQREVIYG QRYEVITTEE SLDEIILGMI ERVISNLVAD NTAGLEREEY KLKNIVEYVD ANLLSETKIN QADLENKDAE QLETYIWEIV QAEYETKRNL LDAEQWLEFE KVVMLRVVDT KWTDHIDAMD HLREGINLRA YGQINPLQEY QAEGYRMFNA MVESVDDDVT RYVMKAEIRQ NLEREQVAKG NAVSGEQTEK VAKKMPTQKD QHIGRNDSCP CGSGKKI //