SECA_CAUSK
ID SECA_CAUSK Reviewed; 921 AA.
AC B0SVL4;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 08-APR-2008, sequence version 1.
DT 03-AUG-2022, entry version 82.
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=Caul_0922;
OS Caulobacter sp. (strain K31).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Caulobacterales;
OC Caulobacteraceae; Caulobacter; unclassified Caulobacter.
OX NCBI_TaxID=366602;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K31;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Bruce D., Goodwin L., Thompson L.S., Brettin T.,
RA Detter J.C., Han C., Schmutz J., Larimer F., Land M., Hauser L.,
RA Kyrpides N., Kim E., Stephens C., Richardson P.;
RT "Complete sequence of chromosome of Caulobacter sp. K31.";
RL Submitted (JAN-2008) 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: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: 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:0000255|HAMAP-Rule:MF_01382}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC Rule:MF_01382}; Peripheral membrane protein {ECO:0000255|HAMAP-
CC Rule:MF_01382}; Cytoplasmic side {ECO:0000255|HAMAP-Rule:MF_01382}.
CC Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01382}. Note=Distribution is 50-
CC 50. {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; CP000927; ABZ70053.1; -; Genomic_DNA.
DR RefSeq; WP_012284987.1; NC_010338.1.
DR AlphaFoldDB; B0SVL4; -.
DR SMR; B0SVL4; -.
DR STRING; 366602.Caul_0922; -.
DR PRIDE; B0SVL4; -.
DR EnsemblBacteria; ABZ70053; ABZ70053; Caul_0922.
DR KEGG; cak:Caul_0922; -.
DR eggNOG; COG0653; Bacteria.
DR HOGENOM; CLU_005314_3_0_5; -.
DR OMA; MVHYDVQ; -.
DR OrthoDB; 212453at2; -.
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; 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 3: Inferred from homology;
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..921
FT /note="Protein translocase subunit SecA"
FT /id="PRO_1000087309"
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 512
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
FT BINDING 905
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
FT BINDING 907
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
FT BINDING 916
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
FT BINDING 917
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
SQ SEQUENCE 921 AA; 103598 MW; 7352257C591BAD3D CRC64;
MLGFAKKFFG SSNERKVKAM SARVAQINAL EPEYAALSDE ALKAKTEEFK ARLAKGEPLD
SLLVEAFAVV REAGKRVLGM RHFDVQMVGG MVLHGGGISE MRTGEGKTLV ATLPTYLNAL
EGKGVHVITV NDYLAKRDAE WMGQIHNFLG LSYGVIVNGL SQGERQRAYR SDITYGTNNE
FGFDYLRDNL VYSVEEMVQR GHHYVIVDEV DSILIDEART PLIISGPTED RSEFYKTIDV
LVKDLIKDKT NFDHDEKQKQ VILTEEGQER IEEILMAGGH LAEDTAGLYD AANISIVHHV
NQALRANVLY TFDKDYIVKD DEVILIDEFT GRMMTGRRLS EGLHQAIEAK EGVSVQPENQ
TLASVTIQNY FRLYKKLAGM TGTAATEAQE FDDIYKMGVS EIPTNRPVLR IDDDDEVYRT
EREKNDSILK QITDCHARGQ PILVGTVSIE KSEELSRLLA TYAWEWEGKK HTGIPHQVLN
ARFHEQEAGI VADAGVPGAV TIATNMAGRG TDIQLGGNMD MRLANWRQQQ KGLGITPTHE
DELAQRAELE IEIGAAKARA LAAGGLFVLG TERHESRRID NQLRGRTGRQ GDPGRSKFFL
SCEDDLLRIF AGERLDAIMR TFGVQEGEAI THKWLNNAIA TAQKRVEQRN YEIRKNLLKY
DDVVNDQRKA VFEQRQEFME ATDLSDIITE MRHDVIDDFI ARYMPPKAYA EQWDIEGLDE
RVQAILGLTL PLKEWAAEEG FGDEEMRERL NKAADEYAAQ REAIITPEQM RSVEKNFLLQ
MIDLQWREHL MHLDHLRNVI GLRGYGQRDP LNEYKTEAFS LFEKLLGDLR TNTTRWLMTV
EIAYAEPEPL HTPEGLVEVH LDPLSGENVA TAGALPEGLS PQQREALPVS VLPEGWEYTA
RNGACPCGSG KKFKHCHGAL V
