SECA_RHOCA
ID SECA_RHOCA Reviewed; 904 AA.
AC P52966;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 97.
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};
OS Rhodobacter capsulatus (Rhodopseudomonas capsulata).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC Rhodobacteraceae; Rhodobacter.
OX NCBI_TaxID=1061;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], SUBUNIT, IN VITRO TRANSLOCATION, AND
RP SUBCELLULAR LOCATION.
RC STRAIN=DSM 938 / 37b4;
RX PubMed=9190818; DOI=10.1128/jb.179.12.4003-4012.1997;
RA Helde R., Wiesler B., Wachter E., Neubueser A., Hoffschulte H.K.,
RA Hengelage T., Schimz K.-L., Stuart R.A., Mueller M.;
RT "Comparative characterization of SecA from the alpha-subclass purple
RT bacterium Rhodobacter capsulatus and Escherichia coli reveals differences
RT in membrane and precursor specificity.";
RL J. Bacteriol. 179:4003-4012(1997).
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: Part of the essential protein translocation apparatus which
CC comprises SecA, SecYEG and auxiliary proteins SecDF-YajC and YidC (By
CC similarity). Homodimer. {ECO:0000250, ECO:0000269|PubMed:9190818}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC Rule:MF_01382, ECO:0000269|PubMed:9190818}; Peripheral membrane protein
CC {ECO:0000255|HAMAP-Rule:MF_01382, ECO:0000269|PubMed:9190818};
CC Cytoplasmic side {ECO:0000255|HAMAP-Rule:MF_01382,
CC ECO:0000269|PubMed:9190818}. Cytoplasm {ECO:0000255|HAMAP-
CC Rule:MF_01382, ECO:0000269|PubMed:9190818}. Note=SecA is found
CC predominantly with the membrane fraction.
CC -!- SIMILARITY: Belongs to the SecA family. {ECO:0000255|HAMAP-
CC Rule:MF_01382}.
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DR EMBL; X89411; CAA61591.1; -; Genomic_DNA.
DR RefSeq; WP_074554294.1; NZ_FNAY01000011.1.
DR AlphaFoldDB; P52966; -.
DR SMR; P52966; -.
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; 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; 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 PANTHER; PTHR30612; PTHR30612; 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; 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 1: Evidence at protein level;
KW ATP-binding; Cell inner membrane; Cell membrane; Cytoplasm; Membrane;
KW Metal-binding; Nucleotide-binding; Protein transport; Translocase;
KW Translocation; Transport; Zinc.
FT CHAIN 1..904
FT /note="Protein translocase subunit SecA"
FT /id="PRO_0000109600"
FT REGION 872..892
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 89
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
FT BINDING 107..111
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
FT BINDING 502
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
FT BINDING 888
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
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 899
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
FT BINDING 900
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
SQ SEQUENCE 904 AA; 101099 MW; 1902B98952BD3C62 CRC64;
MLGLGYIGRK LFGTPNDRKV KRTRPLVAKI NALEPAFEKL SDAEIVAKTR ELQARAQAGE
SLDALLVEAF ANCREAARRA LGLRAFDTQL MGGIFLHQGN IAEMKTGEGK TLVATFPAYL
NALAGKGVHI VTVNDYLARR DSEWMGKVYR HLGLTCGVVY PFQPDDEKRA AYGADITYAT
NNELGFDYLR DNMKSSVAEM YQRDHFFAIV DEVDSILIDE ARTPLIISGP SQDRSDMYRT
LDAYIPFLTE EHYKLDEKQR NATFTEEGNE FLEQKLQADG LLPEGQSLYD PESTTIVHHI
GQALRAHKLF FKDQNYVVTD DEIVLIDEFT GRMMKGRRLS DGLHQAIEAK ERVTIQPENV
TLASVTFQNY FRLYEKLAGM TGTAVTEAEE FGDIYKLGVV EVPTNRPVAR KDEHDRVYRT
AKEKYAAVIE AIKTAHEKGQ PTLVGTTSIE KSEMLSEMLK AEGLPHNVLN ARQHEQEAQI
VADAGRLGAI TIATNMAGRG TDIQLGGNVE MKVQEEIAAN PEAAPEEIRA RIEAEHAAEK
QKVIEAGGLF VLATERHESR RIDNQLRGRS GRQGDPGRSL FFLSLEDDLM RIFGSDRLEG
VLSKLGMKEG EAIIHPWVNK SLERAQAKVE GRNFDWRKQL LKFDDVMNDQ RKAVFGQRRE
IMETDEISEI VADMRQQVID DLIDDFAPPK SYVDQWDIEG MRAAFIDHAG VDLPLADWAA
EEGVDQDVLR ERVTAALDAV MAQKTEAFGA ETMRVIEKQI LLQTIDAKWR EHLVTLEHLR
SVVGFRGYAQ RDPLSEYKTE SFQLFESMLD SLRYEVTKRL GQIRPMSDEE RAEMLRQQAA
ALAAAEGAAD PAEAPAPQPA AQVALAAAPG FVESDPTTWG EPSRNDPCPC GSGEKFKHCH
GRLA
