ID A0A1V4HUG1_NITVU Unreviewed; 806 AA. AC A0A1V4HUG1; DT 07-JUN-2017, integrated into UniProtKB/TrEMBL. DT 07-JUN-2017, sequence version 1. DT 10-OCT-2018, entry version 9. DE RecName: Full=Protein translocase subunit SecA {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; Rhizobiales; 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 RT vulgaris strain Ab1."; RL Submitted (FEB-2017) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Part of the Sec protein translocase complex. Interacts CC with the SecYEG preprotein conducting channel. Has a central role CC in coupling the hydrolysis of ATP to the transfer of proteins into CC and across the cell membrane, serving both as a receptor for the CC preprotein-SecB complex and as an ATP-driven molecular motor CC driving the stepwise translocation of polypeptide chains across CC the membrane. {ECO:0000256|HAMAP-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- CC Rule:MF_01382}; Peripheral membrane protein {ECO:0000256|HAMAP- CC Rule:MF_01382}; Cytoplasmic side {ECO:0000256|HAMAP- CC Rule:MF_01382}. Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01382}. CC Note=Distribution is 50-50. {ECO:0000256|HAMAP-Rule:MF_01382}. CC -!- SIMILARITY: Belongs to the SecA family. {ECO:0000256|HAMAP- CC Rule:MF_01382}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {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 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 HAMAP; MF_01382; SecA; 1. 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; 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; 3. DR SUPFAM; SSF81767; SSF81767; 1. DR SUPFAM; SSF81886; SSF81886; 1. DR PROSITE; PS51196; SECA_MOTOR_DEAD; 1. PE 3: Inferred from homology; KW ATP-binding {ECO:0000256|HAMAP-Rule:MF_01382}; KW Cell membrane {ECO:0000256|HAMAP-Rule:MF_01382}; KW Complete proteome {ECO:0000313|Proteomes:UP000189940}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01382}; KW Membrane {ECO:0000256|HAMAP-Rule:MF_01382}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01382}; KW Protein transport {ECO:0000256|HAMAP-Rule:MF_01382}; KW Translocation {ECO:0000256|HAMAP-Rule:MF_01382}; KW Transport {ECO:0000256|HAMAP-Rule:MF_01382}. FT DOMAIN 3 599 SECA_MOTOR_DEAD. {ECO:0000259|PROSITE: FT PS51196}. FT NP_BIND 102 109 ATP. {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 //