SECA_DEIRA
ID SECA_DEIRA Reviewed; 868 AA.
AC Q9RWU0;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 26-FEB-2008, sequence version 2.
DT 03-AUG-2022, entry version 124.
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=DR_0575;
OS Deinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / LMG
OS 4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422).
OC Bacteria; Deinococcus-Thermus; Deinococci; Deinococcales; Deinococcaceae;
OC Deinococcus.
OX NCBI_TaxID=243230;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB
RC 9279 / R1 / VKM B-1422;
RX PubMed=10567266; DOI=10.1126/science.286.5444.1571;
RA White O., Eisen J.A., Heidelberg J.F., Hickey E.K., Peterson J.D.,
RA Dodson R.J., Haft D.H., Gwinn M.L., Nelson W.C., Richardson D.L.,
RA Moffat K.S., Qin H., Jiang L., Pamphile W., Crosby M., Shen M.,
RA Vamathevan J.J., Lam P., McDonald L.A., Utterback T.R., Zalewski C.,
RA Makarova K.S., Aravind L., Daly M.J., Minton K.W., Fleischmann R.D.,
RA Ketchum K.A., Nelson K.E., Salzberg S.L., Smith H.O., Venter J.C.,
RA Fraser C.M.;
RT "Genome sequence of the radioresistant bacterium Deinococcus radiodurans
RT R1.";
RL Science 286:1571-1577(1999).
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF10155.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AE000513; AAF10155.1; ALT_INIT; Genomic_DNA.
DR PIR; D75501; D75501.
DR RefSeq; NP_294298.2; NC_001263.1.
DR RefSeq; WP_010887220.1; NZ_CP015081.1.
DR AlphaFoldDB; Q9RWU0; -.
DR SMR; Q9RWU0; -.
DR STRING; 243230.DR_0575; -.
DR PRIDE; Q9RWU0; -.
DR EnsemblBacteria; AAF10155; AAF10155; DR_0575.
DR KEGG; dra:DR_0575; -.
DR PATRIC; fig|243230.17.peg.753; -.
DR eggNOG; COG0653; Bacteria.
DR HOGENOM; CLU_005314_3_2_0; -.
DR InParanoid; Q9RWU0; -.
DR OMA; MVHYDVQ; -.
DR OrthoDB; 212453at2; -.
DR Proteomes; UP000002524; Chromosome I.
DR GO; GO:0031522; C:cell envelope Sec protein transport complex; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0015462; F:ABC-type protein transporter activity; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IBA:GO_Central.
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 GO; GO:0043952; P:protein transport by the Sec complex; IBA:GO_Central.
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; 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..868
FT /note="Protein translocase subunit SecA"
FT /id="PRO_0000320792"
FT BINDING 85
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
FT BINDING 103..107
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
FT BINDING 508
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
SQ SEQUENCE 868 AA; 97270 MW; D534956812FF1AE1 CRC64;
MFRVLNKVFD NNKRDVERII QTVVKPVNAL EEETMRVENL AEAFMDLRRR VQDGGESLDS
LIVPAFALIR EAGRRSIGKR HYDTQLIGGA ALHQGRIAEM RTGEGKTLVA TLALAFNALE
GKGCHLVTVN DYLARVGMEE MGLLYRTLGL TVGLANRELS PAEKQAAYAC DITYVTNSEL
GFDYLRDNMA QSKEALVLRA DTPLHYAIVD EVDSILIDEA RTPLIISGAA EKATDLYYVF
AKLIRRLQKG EPAEPGVRTE PTGDYTIEEK SKAVHLTEQG ITKIERLLSL KDLYSPENMD
KAHMITQAIR ARELYHREKD YIVNAEGEVV IVDEFTGRSM PGRRYGEGLH QAIEAKEGVK
IENENQTLAT ITYQNFFRLY DKFAGMTGTA KTEEKEFLDI YGSDVLVIPT NKPVIRVDSD
DLIYRTRMGK YAAVVGEVQE MHATGRPILI GTASIETSEQ LSSLLQQAGV QHAVLNAKFE
AQEASIIAQA GRSGTVTIAT NMAGRGTDIM LGGNDEYIIG ESIEQQLGVS RYAPEVEAFI
KAISREDPAA EQLGMQIPGI TLDFIRQAQE LHRATVEDRQ RVRDLGGLHI VGTERHESRR
IDNQLRGRAG RQGDPGSSRF YVSFEDDLMR LFANDRVVGM MDRLGMDDSQ PIEAKMVTGA
IEKAQARVED RNFGIRKQLL EFDNVMSKQR DEIYAQRREV LLGPDEDIEE TTEGMIGDFV
DSQLAAYAPI EVSHEQWDIE QLRSAMVEAV PALETFDFES LRVNSPAEAQ DRLLSAVADA
FDARKEELSP TMMNSLARYV LLQVVDQHWK EHLHGMDVLR QGIGLRGYGQ RDPFTEYKFE
ATNMFNEMID ALKADVTKFI FRMQFGGA
