ID A0A1V4HUG1_NITVU Unreviewed; 806 AA. AC A0A1V4HUG1; DT 07-JUN-2017, integrated into UniProtKB/TrEMBL. DT 07-JUN-2017, sequence version 1. DT 25-MAY-2022, entry version 34. 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 ORFNames=B2M20_16605 {ECO:0000313|EMBL:OPH81631.1}; OS Nitrobacter vulgaris. OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales; OC Bradyrhizobiaceae; Nitrobacter. OX NCBI_TaxID=29421 {ECO:0000313|EMBL:OPH81631.1, ECO:0000313|Proteomes:UP000189940}; RN [1] {ECO:0000313|EMBL:OPH81631.1, ECO:0000313|Proteomes:UP000189940} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Ab1 {ECO:0000313|EMBL:OPH81631.1, RC ECO:0000313|Proteomes:UP000189940}; RA Mellbye B.L., Davis E.W., Spieck E., Chang J.H., Bottomley P.J., RA Sayavedra-Soto L.A.; RT "Genome sequence of the nitrite-oxidizing bacterium Nitrobacter vulgaris RT strain Ab1."; RL Submitted (FEB-2017) 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 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:0000256|HAMAP-Rule:MF_01382}. CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + H(2)O + cellular protein(Side 1) = ADP + phosphate + CC cellular protein(Side 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-YajC and YidC. {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 -!- 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:OPH81631.1}. 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; MWPQ01000056; OPH81631.1; -; Genomic_DNA. DR STRING; 29421.B2M20_16605; -. DR EnsemblBacteria; OPH81631; OPH81631; B2M20_16605. DR Proteomes; UP000189940; 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; cd18803; SF2_C_secA; 1. DR Gene3D; 3.40.50.300; -; 3. DR HAMAP; MF_01382; SecA; 1. DR InterPro; IPR014001; Helicase_ATP-bd. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR000185; SecA. 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; PTHR30612; 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; SSF52540; SSF52540; 2. DR SUPFAM; SSF81767; SSF81767; 1. DR SUPFAM; SSF81886; SSF81886; 1. DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 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}; Cytoplasm {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:UP000189940}; 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 3..599 FT /note="SECA_MOTOR_DEAD" FT /evidence="ECO:0000259|PROSITE:PS51196" FT DOMAIN 89..262 FT /note="Helicase ATP-binding" FT /evidence="ECO:0000259|PROSITE:PS51192" FT NP_BIND 105..109 FT /note="ATP" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01382" FT BINDING 87 FT /note="ATP" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01382" FT BINDING 512 FT /note="ATP" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01382" SQ SEQUENCE 806 AA; 89106 MW; D0B912295640BD6A CRC64; MIPRLARRAL SFGTRRKLTQ YETTADRILA QESDCRRLSS GGLLDRVAEL RRRVQAGSAI DGIKQEAFAL AREAAWRALS EHPVPVQIIG ALALHDGHLA EMKTGEGKTL TAALVCALNA LTGRGVHVAT PNDYLAERDA AWMRPFYDLL GLSTGVITQE MDDDSRREAY RCDITYGIAS EFGFDYLRDN LKFSAAETVQ RGHAFALVDE ADATLIDEAS MPLALFGPLG DHSGFYHAID AEVASLQPSH YEIDHRRRVA LTEAGYSEIE LRLQQQRLLK ASTTLHDIAS ISLLHHVMQS LRAHVMLARD RDYVVENGSV TIVDRLTGRP MPGRRYDEGL HQALEAKEGC AIGEETRTLA SITFQTYFQR YAKLSGMTGT AKADTEEYRD IYGLDVISIP THRPMIRVDE TVLHSTAAGK FQAILRELED AAARGQPVLI GVPSIERSEA LAAMLEANGW RQQNAPAQNP GSSRTFSVLN AKHHAREAQI IAEAGAPGAV TIATAMAGRG TDIRLGGEHA DALTRARVIA AGGLLVIGTT HHDHGRMDEQ LRGRAGRQGD PGRSVIHASL QDEFLRTAAI NAPPTLLTEQ AATIAPSVAT LLIEAAQKRH EMRSFDRRLG LLRFDTIIQR QRDNVFDLRQ SIRDGSDTLM LVKRLRHETV DDLINRFATP TAPWDIAGLD HAIRSVLTLA IDIRPPSSDP KADAKVLTQL ITAAADRWID GKIASMGETM FIDILRRLMM ALIDHLWSEQ SERLDHLKRR IGDRGLPPHK VVAEFQLEAF ALFERMIVDF RRDVTAYSMR VGILPS //