ID A0A975A2A1_9BACT Unreviewed; 1114 AA. AC A0A975A2A1; DT 22-FEB-2023, integrated into UniProtKB/TrEMBL. DT 22-FEB-2023, sequence version 1. DT 27-MAR-2024, entry version 7. DE RecName: Full=Protein translocase subunit SecA {ECO:0000256|HAMAP-Rule:MF_01382}; DE EC=7.4.2.8 {ECO:0000256|HAMAP-Rule:MF_01382}; GN Name=secA {ECO:0000256|HAMAP-Rule:MF_01382, GN ECO:0000313|EMBL:QSE98621.1}; GN ORFNames=JR347_05960 {ECO:0000313|EMBL:QSE98621.1}; OS Fulvivirga lutea. OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Fulvivirgaceae; OC Fulvivirga. OX NCBI_TaxID=2810512 {ECO:0000313|EMBL:QSE98621.1, ECO:0000313|Proteomes:UP000662783}; RN [1] {ECO:0000313|EMBL:QSE98621.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=S481 {ECO:0000313|EMBL:QSE98621.1}; RA Bae S.S., Baek K.; RT "Fulvivirga sp. S481 isolated from sea water."; RL Submitted (FEB-2021) 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}. 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; CP070608; QSE98621.1; -; Genomic_DNA. DR KEGG; fuv:JR347_05960; -. DR Proteomes; UP000662783; 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: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:SF0; CHLOROPLAST PROTEIN-TRANSPORTING ATPASE; 1. DR PANTHER; PTHR30612; SECA INNER MEMBRANE COMPONENT OF SEC PROTEIN SECRETION SYSTEM; 1. DR Pfam; PF21090; P-loop_SecA; 2. 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}; Cell inner membrane {ECO:0000256|ARBA:ARBA00022519}; 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:UP000662783}; 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 2..771 FT /note="SecA family profile" FT /evidence="ECO:0000259|PROSITE:PS51196" FT DOMAIN 178..337 FT /note="Helicase ATP-binding" FT /evidence="ECO:0000259|PROSITE:PS51192" FT DOMAIN 618..770 FT /note="Helicase C-terminal" FT /evidence="ECO:0000259|PROSITE:PS51194" FT REGION 717..736 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1026..1072 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1030..1050 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 176 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01382" FT BINDING 194..198 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01382" FT BINDING 693 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01382" SQ SEQUENCE 1114 AA; 127260 MW; AC1EA5A39AB3FD07 CRC64; MLKFIAKVFG TKSDKDIKKL MPMVEEINAE FAKLSSISDQ ELREKSRAVK GDIDEYLKSI DEEIASLHQK VNDNPDLDIH EKEEIFNQID SLEEKRNKDL EEVLLKVLPR AFAIVKETAR RFKDNDQLEV VATMHDKTLA AKKPNVEIDG DKAIWKNKWL AAGTEIKWDM LHYDEQLIGG IVLHEGKIAE MATGEGKTLV ATLPAFLNAL AKRGVHVVTV NDYLAKRDSE WMAPIFEFHE LTVDCIDKHE PNSEERKTAY GCDIIYGTNN EFGFDYLRDN MSRETDDLVQ KKHHYAMIDE VDSVLIDEAR TPLIISGPVP RGDEHEFYDL KPRISKLVDA QKKLTQQFLV EAKKLISEGN EKEGGLALFR AYRGLPKHKP LIKYLSETGM RQILQKTENF YLQDNQKMMP EADEPLYFTI DEKHNSIELT EKGIDLITKE GEDSNFFIMP DIGVEIANLE KDEALTDEEK VAKKDELIKD YSIKSQRIHS VNQLLKAYTL FEKDTEYIIV DGKVKIVDEQ TGRVMDGRRY SDGLHQAIEA KENVKVEDAT QTYATITLQN YFRMYHKLAG MTGTAETEAG EFWEIYKLDV VVMPTHRPIA RDDKQDMVYK TVREKFNAVV DEIVALTEKG RPVLVGTTSV EISELVSRML NMRKINHQVL NAKQHAREAE VVAEAGKPGT VTIATNMAGR GTDIKLTPES KAAGGLAIIG TERHESRRVD RQLRGRSGRQ GDPGSSQFFV SLEDNLMRMF MPERIARIMD KLGLQEGEVI SHSMVTKSIE RAQTKVEENN FGIRKRLLEY DDVMNSQREV IYKRRRNALY GERLQLDIMN MLFDTCEDIV LNTKGADNYD SFKLTVLGVL GVDFEITKDE FSSISEENLT QKLYDVAYEA YKRKNNGIAE KALPIIKNIS ETRGATIENI LIPFTDGKKQ IGVAANLQKC VDTNNKEMIK SMEKMITLAI IDQLWKDHLR EMDDLKQSVQ NAVYEQKDPL LIYKFEGFEL FKRFIAKVNE DTISFLMKAD LPVEDPNQVQ EARQRGRQKL SEKKEESRSL LSGGRQPAAN RPPAEITKPL KSEKVFGRND RVTVQYMDGS MKKDVKFKTV EADINNNKCV LVED //