SECA_PAEAT
ID SECA_PAEAT Reviewed; 913 AA.
AC A1R844;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2007, sequence version 1.
DT 03-AUG-2022, entry version 116.
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=AAur_2691;
OS Paenarthrobacter aurescens (strain TC1).
OC Bacteria; Actinobacteria; Micrococcales; Micrococcaceae; Paenarthrobacter.
OX NCBI_TaxID=290340;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TC1;
RX PubMed=17194220; DOI=10.1371/journal.pgen.0020214;
RA Mongodin E.F., Shapir N., Daugherty S.C., DeBoy R.T., Emerson J.B.,
RA Shvartzbeyn A., Radune D., Vamathevan J., Riggs F., Grinberg V.,
RA Khouri H.M., Wackett L.P., Nelson K.E., Sadowsky M.J.;
RT "Secrets of soil survival revealed by the genome sequence of Arthrobacter
RT aurescens TC1.";
RL PLoS Genet. 2:2094-2106(2006).
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: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 -!- 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:0000255|HAMAP-Rule:MF_01382}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|HAMAP-Rule:MF_01382};
CC Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_01382};
CC Cytoplasmic side {ECO:0000255|HAMAP-Rule:MF_01382}. Cytoplasm
CC {ECO:0000255|HAMAP-Rule:MF_01382}. Note=Distribution is 50-50.
CC {ECO:0000255|HAMAP-Rule:MF_01382}.
CC -!- SIMILARITY: Belongs to the SecA family. {ECO:0000255|HAMAP-
CC Rule:MF_01382}.
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DR EMBL; CP000474; ABM09519.1; -; Genomic_DNA.
DR RefSeq; WP_011775347.1; NC_008711.1.
DR AlphaFoldDB; A1R844; -.
DR SMR; A1R844; -.
DR STRING; 290340.AAur_2691; -.
DR PRIDE; A1R844; -.
DR EnsemblBacteria; ABM09519; ABM09519; AAur_2691.
DR KEGG; aau:AAur_2691; -.
DR eggNOG; COG0653; Bacteria.
DR HOGENOM; CLU_005314_3_0_11; -.
DR OMA; MVHYDVQ; -.
DR OrthoDB; 212453at2; -.
DR Proteomes; UP000000637; 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: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; cd18803; SF2_C_secA; 1.
DR Gene3D; 3.40.50.300; -; 2.
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; 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 TIGRFAMs; TIGR00963; secA; 1.
DR PROSITE; PS01312; SECA; 1.
DR PROSITE; PS51196; SECA_MOTOR_DEAD; 1.
PE 3: Inferred from homology;
KW ATP-binding; Cell membrane; Cytoplasm; Membrane; Nucleotide-binding;
KW Protein transport; Reference proteome; Translocase; Translocation;
KW Transport.
FT CHAIN 1..913
FT /note="Protein translocase subunit SecA"
FT /id="PRO_0000318307"
FT REGION 865..913
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 86
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
FT BINDING 104..108
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
FT BINDING 494
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
SQ SEQUENCE 913 AA; 101694 MW; B14DF9AEABE86308 CRC64;
MASLIEKLLR TGDKKTLKTL RNYADSINAL EDTFKSFTDA EIREETDRLR SRHQDGETLE
ALLPEAFAAV REASSRTLGM RHFDVQLMGG AALHLGNIAE MKTGEGKTLV ATAPAYLNAL
SGKGVHVVTV NDYLAEYQSE LMGRVYRFLG LTSGCILSNQ DPTVRREQYA ADITYGTNNE
FGFDYLRDNM AWDAGELVQR GHNFAIVDEV DSILIDEART PLIISGPAQG DTNRWYSEFS
KVVLRLQPDV DYEVDEKKRT VGVLEAGIEK VEDYLGIQNL YESANTPLIG FLNNAIKAKE
LFKRDKDYVI LDGEVLIVDE HTGRILAGRR YNEGMHQAIE AKENVEIKAE NQTLATVTLQ
NYFRMYSKLA GMTGTAETEA AEFMSTYKLG VVPIPTNRDM QRIDQSDLVY KNEVVKFDAV
VQDIAERHKN GQPVLVGTTS VEKSEYLSKL LAKEGIRHEV LNAKNHAREA SIVAQAGRKG
AVTVATNMAG RGTDIMLGGN AEFTAIAELS KRGLDPEENS DEYEAAWPAA LAAAKQAVKD
EHEEVLDLGG LYVLGTERHE SRRIDNQLRG RSGRQGDPGE SRFYLSLTDD LMRLFNSGAA
ERLMNSSVPD DVALESKLVS RAIASAQGQV EGRNAEQRKN VLKYDDVLNR QREAIYGDRR
RILEGDDLHE KVQYFLEDTI NSLIDAATAE GSGDDWDYNQ LWANLRTLYP ATVTAQEIID
EAGGKSRVTA EFLREEILSD ARLVYQAREE AIGSESMREL ERRVVLSVIG RKWQEHLYEM
DYLKEGIGLR AMAQRDPLVE YQREGFVMFQ SMMEAIREES IGFLYNLEVE VTPAEDVVVA
DGSAAGAHTE HHDPQIRAAG LEAPEKPAQL QYTAPGEDGG TQTRIEGRAS GRSGNPAKAA
SQEPRKQAKK KRR
