SECA_CAUVN
ID SECA_CAUVN Reviewed; 923 AA.
AC B8H392; P38380;
DT 16-JUN-2009, integrated into UniProtKB/Swiss-Prot.
DT 03-MAR-2009, sequence version 1.
DT 03-AUG-2022, entry version 84.
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=CCNA_03164;
OS Caulobacter vibrioides (strain NA1000 / CB15N) (Caulobacter crescentus).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Caulobacterales;
OC Caulobacteraceae; Caulobacter.
OX NCBI_TaxID=565050;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8051008; DOI=10.1128/jb.176.16.4958-4965.1994;
RA Kang P.J., Shapiro L.;
RT "Cell cycle arrest of a Caulobacter crescentus secA mutant.";
RL J. Bacteriol. 176:4958-4965(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NA1000 / CB15N;
RX PubMed=20472802; DOI=10.1128/jb.00255-10;
RA Marks M.E., Castro-Rojas C.M., Teiling C., Du L., Kapatral V.,
RA Walunas T.L., Crosson S.;
RT "The genetic basis of laboratory adaptation in Caulobacter crescentus.";
RL J. Bacteriol. 192:3678-3688(2010).
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, ECO:0000305};
CC Note=May bind 1 zinc ion per subunit. {ECO:0000255|HAMAP-Rule:MF_01382,
CC ECO:0000305};
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, ECO:0000305}.
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DR EMBL; U06928; AAA57279.1; -; Genomic_DNA.
DR EMBL; CP001340; ACL96629.1; -; Genomic_DNA.
DR PIR; A55854; A55854.
DR RefSeq; WP_010920904.1; NC_011916.1.
DR RefSeq; YP_002518537.1; NC_011916.1.
DR AlphaFoldDB; B8H392; -.
DR SMR; B8H392; -.
DR PRIDE; B8H392; -.
DR EnsemblBacteria; ACL96629; ACL96629; CCNA_03164.
DR GeneID; 7331002; -.
DR KEGG; ccs:CCNA_03164; -.
DR PATRIC; fig|565050.3.peg.3090; -.
DR HOGENOM; CLU_005314_3_0_5; -.
DR OMA; MVHYDVQ; -.
DR OrthoDB; 212453at2; -.
DR PhylomeDB; B8H392; -.
DR Proteomes; UP000001364; 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: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 3: Inferred from homology;
KW ATP-binding; Cell inner membrane; Cell membrane; Cytoplasm; Membrane;
KW Metal-binding; Nucleotide-binding; Protein transport; Reference proteome;
KW Translocase; Translocation; Transport; Zinc.
FT CHAIN 1..923
FT /note="Protein translocase subunit SecA"
FT /id="PRO_0000378310"
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 906
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
FT BINDING 908
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"
FT BINDING 918
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
FT CONFLICT 26..35
FT /note="KINAYEAEYA -> RSTPMKPNT (in Ref. 1; AAA57279)"
FT /evidence="ECO:0000305"
FT CONFLICT 278..280
FT /note="GGH -> AAN (in Ref. 1; AAA57279)"
FT /evidence="ECO:0000305"
FT CONFLICT 290..291
FT /note="DA -> RR (in Ref. 1; AAA57279)"
FT /evidence="ECO:0000305"
FT CONFLICT 310
FT /note="Y -> I (in Ref. 1; AAA57279)"
FT /evidence="ECO:0000305"
FT CONFLICT 521..522
FT /note="MR -> IA (in Ref. 1; AAA57279)"
FT /evidence="ECO:0000305"
FT CONFLICT 528..529
FT /note="QQ -> HE (in Ref. 1; AAA57279)"
FT /evidence="ECO:0000305"
FT CONFLICT 593..595
FT /note="PGR -> RS (in Ref. 1; AAA57279)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 923 AA; 103939 MW; 15D0C840A658780D CRC64;
MLGFAKKLFG SSNERKVKTL ATRVAKINAY EAEYAALSDE ALKGKTAEFK ARLEKGETLD
DILNEAFAVV REASKRVLGM RHFDVQMVGG MVLHFSGISE MRTGEGKTLV ATLPTYLNAL
EGKGVHVITV NDYLARRDAD WMGQVYNFLG LSYGVIVNGL SQGERQRAYR SDITYGTNNE
FGFDYLRDNL VYSVDEMVQR GHNFAIVDEV DSILIDEART PLIISGPTED RSSFYKTIDV
LVKELILDKS MFDHDEKQKQ VILTEDGQEK IEEILMSGGH LAEDSAGLYD AANVSVVHHV
NQALRANILY TRDKDYIVKG GEVVLIDEFT GRMMTGRRLS EGLHQAIEAK EGADIQPENQ
TLASVTIQNY FRLYKKLSGM TGTASTEAQE FDDIYKMSVS EIPTNRTIQR IDDDDEVYRT
EREKNEAILK QIADCHVRGQ PILVGTVSIE KSEELSKLLS TFSFEKDGKK VKGIPHQVLN
ARFHEQEAVI VADAGVPGAV TIATNMAGRG TDIQLGGSID MRLFNWRQQQ RGMGLEITVE
DEAEERARLE TEIADKKAQA LAAGGLFVLG TERHESRRID NQLRGRTGRQ GDPGRSKFFL
SCEDDLLRIF AGERLDAIMR TFGVQEGEAI THKWLNNAIA TAQKRVEQRN YEIRKNLLKY
DDVVNDQRKA VFEQRQEFME SSDLSDIIHE MRRDVIDDLV LRHLPPKAYA EQWDVEGLTE
RVKSILGLDL PIAEWAAEEG IADEEMKERI TKAADEYAAQ REVIITPEQM RSVEKSFLLQ
MIDLQWREHL MHLDHLRNVI GLRGYGQRDP LNEYKTEAFS LFEKLLGDLR TNTTRWLMTV
EIAYAEPEVP HTPLDNLVEV HLDPLTGENA AFAGGIPEGL STAQREALPV SALPEGWDRT
NRNAPCPCGS GKKFKQCHGS LVR
