ID SECA_LARHH Reviewed; 906 AA. AC C1D5K2; DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot. DT 26-MAY-2009, sequence version 1. DT 24-JAN-2024, entry version 78. 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=LHK_03041; OS Laribacter hongkongensis (strain HLHK9). OC Bacteria; Pseudomonadota; Betaproteobacteria; Neisseriales; OC Aquaspirillaceae; Laribacter. OX NCBI_TaxID=557598; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=HLHK9; RX PubMed=19283063; DOI=10.1371/journal.pgen.1000416; RA Woo P.C.Y., Lau S.K.P., Tse H., Teng J.L.L., Curreem S.O., Tsang A.K.L., RA Fan R.Y.Y., Wong G.K.M., Huang Y., Loman N.J., Snyder L.A.S., Cai J.J., RA Huang J.-D., Mak W., Pallen M.J., Lok S., Yuen K.-Y.; RT "The complete genome and proteome of Laribacter hongkongensis reveal RT potential mechanisms for adaptations to different temperatures and RT habitats."; RL PLoS Genet. 5:E1000416-E1000416(2009). 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 both as a receptor for the CC preprotein-SecB complex and as an ATP-driven molecular motor driving CC the stepwise translocation of polypeptide chains across the membrane. CC {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 -!- 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-Rule:MF_01382}. CC Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01382}. Note=Distribution is 50- CC 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; CP001154; ACO76019.1; -; Genomic_DNA. DR RefSeq; WP_012698482.1; NC_012559.1. DR AlphaFoldDB; C1D5K2; -. DR SMR; C1D5K2; -. DR STRING; 557598.LHK_03041; -. DR GeneID; 75108253; -. DR KEGG; lhk:LHK_03041; -. DR eggNOG; COG0653; Bacteria. DR HOGENOM; CLU_005314_3_0_4; -. DR OMA; MVHYDVQ; -. DR Proteomes; UP000002010; 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:0046872; F:metal ion binding; IEA:UniProtKB-KW. 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; 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; 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; 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; 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; PS01312; SECA; 1. DR PROSITE; PS51196; SECA_MOTOR_DEAD; 1. PE 3: Inferred from homology; KW ATP-binding; Cell inner membrane; Cell membrane; Cytoplasm; Membrane; KW Metal-binding; Nucleotide-binding; Protein transport; Reference proteome; KW Translocase; Translocation; Transport; Zinc. FT CHAIN 1..906 FT /note="Protein translocase subunit SecA" FT /id="PRO_1000184234" FT BINDING 87 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01382" FT BINDING 105..109 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01382" FT BINDING 507 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01382" FT BINDING 890 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01382" FT BINDING 892 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01382" FT BINDING 901 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01382" FT BINDING 902 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01382" SQ SEQUENCE 906 AA; 101119 MW; E9BBD672BC1FC6DC CRC64; MIANILKKVF GSRNDRLLKQ YRAVVNRINA LESGLQTLDD AALAGKTAEF RARVEKGERL DSLLPEAFAV CREASRRVMG MRHFDVQLIG GMVLHDGKIA EMRTGEGKTL VATLPAYLNA LAGKGVHVVT VNDYLASRDA GIMAPLYNFL GLSVGVNLSQ MPHDAKQDAY AADITYGTNN EFGFDYLRDN MVYSPAERVQ KPLSFAIVDE VDSILIDEAR TPLIISGPAD DNVDMYRRMN AIPALLVRQQ AEDGEGDYWV DEKAHTVMLS EAGFEHAEAA LVAADLLKEG ESLYSAANIT LMHHLMAALR AHALFHRDQH YVVQDGEIVI VDEFTGRLMA GRRWSEGLHQ AVEAKEGVNI NRENQTLASI TFQNYFRLYK KLAGMTGTAD TEAYEFQQIY GLETVVIPTN RPMVRKDSLD LVYRTGQEKY NAILADITDC HQRGQPVLVG TTSIENSELL AGLLKQAGLP HNVLNAKEHA READIIVQAG RPGVVTVATN MAGRGTDIVL GGNIAPEIKA IESDESLTAD DRAQRIAALK AEWQARHDAV LAAGGLHIIG TERHESRRID NQLRGRSGRQ GDPGSSRFYL SLEDPLLRIF ASERVSAIMQ RLNMPEGEAI EHSWVTRAIE NAQRKVEGRN FDIRKQLLEY DDVANDQRRV IYQQRNEILE SEEVSDMIAA MRDDVLSQLF DTWMPPQSIE EQWDAAGLMR VLEADYQISV PLADWIKAEP NAELDTFKIR ILEQARALYD EKVAAVGAAS MQQFERAVLL QHFDGAWREH LAALDHLRQG IHLRGYAQKN PKQEYKREAF ELFSLMLDRI KREVTQIVAT VQIRSPEEAA AAEAFEHEER PMTYRHDEFT VEGDEAGEGN PFTAEKLAAA GVRVGRNDPC PCGSGKRYKQ CHGRLA //