SECA_CAMLR
ID SECA_CAMLR Reviewed; 863 AA.
AC B9KFM5;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-MAR-2009, sequence version 1.
DT 03-AUG-2022, entry version 88.
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=Cla_0525;
OS Campylobacter lari (strain RM2100 / D67 / ATCC BAA-1060).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Campylobacteraceae; Campylobacter.
OX NCBI_TaxID=306263;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RM2100 / D67 / ATCC BAA-1060;
RX PubMed=18713059; DOI=10.1089/fpd.2008.0101;
RA Miller W.G., Wang G., Binnewies T.T., Parker C.T.;
RT "The complete genome sequence and analysis of the human pathogen
RT Campylobacter lari.";
RL Foodborne Pathog. Dis. 5:371-386(2008).
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 -!- 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; CP000932; ACM63860.1; -; Genomic_DNA.
DR RefSeq; WP_012661243.1; NC_012039.1.
DR AlphaFoldDB; B9KFM5; -.
DR SMR; B9KFM5; -.
DR STRING; 306263.Cla_0525; -.
DR PRIDE; B9KFM5; -.
DR EnsemblBacteria; ACM63860; ACM63860; CLA_0525.
DR GeneID; 7411085; -.
DR KEGG; cla:CLA_0525; -.
DR PATRIC; fig|306263.5.peg.509; -.
DR eggNOG; COG0653; Bacteria.
DR HOGENOM; CLU_005314_3_0_7; -.
DR OMA; MVHYDVQ; -.
DR OrthoDB; 212453at2; -.
DR Proteomes; UP000007727; 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; -; 3.
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; 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; 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..863
FT /note="Protein translocase subunit SecA"
FT /id="PRO_1000184221"
FT REGION 806..863
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 812..833
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 88
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
FT BINDING 106..110
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
FT BINDING 507
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
FT BINDING 840
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
FT BINDING 842
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
FT BINDING 851
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
FT BINDING 852
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
SQ SEQUENCE 863 AA; 98657 MW; 271FFE07019DC95D CRC64;
MFSSVFKAIF GTKNDREVKK YLKRVAQINA LESKYQNLSD DELKQKFIDF KTQIQKEEKT
LDQILNDVFA IVREVGKRTL NMRHFDVQLI GGMVLHEGKI AEMKTGEGKT LVATLPVVLN
AMSGKGVHVV TVNDYLAKRD AEQMSAIYNF LGFSVGVILS EQNSDEAHKK AYECDITYGT
NNEFGFDYLR DNMKFSKLEK VQREHHFVIV DEVDSILIDE ARTPLIISGP TNRTLDGYIK
ANEVAKQMQK GQAATTPQEL PSGDFVVDEK NRTIMITEAG ISKAEKLFGV ENLYSLDNAI
LAHQLDQALK AHNLFEKDVH YVLRDKEVVI VDEFTGRLSE GRRFSDGLHQ ALEAKENVKI
QEESQTLADI TFQNYFRMYK KLAGMTGTAQ TEATEFSQIY NLDVVSIPTN IPVARIDKDD
LIYKTQEEKF KAVIEEIKKA NAKGQPVLVG TASIERSEVF HNMLVKERIP HHVLNAKNHE
QEALIIQDAG KKGAVTIATN MAGRGVDIKI DDEVKALGGL YIIGTERHES RRIDNQLRGR
AGRQGDPGVS RFYLSLEDNL LRIFGGDRIK NIMERLGIEE GEHIESRIVT RAVENAQKKV
ESLHFESRKH LLEYDDVANE QRKTIYNYRN ELLDEEFDLQ DKILKNIAEY SNHLVSQIYL
NAELEDDVKH FESLKQKVSY ECNLELNEVD FKDLGVIEVE NKLSEILEKV YKDKMSIIED
KEARRIERIL YLQILDNLWR EHLYQMDILK TGIGLRSYNQ KDPLVEYKKE SYNLFMELVE
RIKFDSLKLL FNVAFTQQQA QNFEEKSHEQ NEQFLSNTTE SGVNENGEAQ ITKVPRNSPC
PCGSGKKYKE CHGKSGPKKG ILA
