SECA_WOLPM
ID SECA_WOLPM Reviewed; 868 AA.
AC Q73HK8;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 26-FEB-2008, sequence version 2.
DT 03-AUG-2022, entry version 119.
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=WD_0549;
OS Wolbachia pipientis wMel.
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC Anaplasmataceae; Wolbachieae; Wolbachia; unclassified Wolbachia.
OX NCBI_TaxID=163164;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15024419; DOI=10.1371/journal.pbio.0020069;
RA Wu M., Sun L.V., Vamathevan J.J., Riegler M., DeBoy R.T., Brownlie J.C.,
RA McGraw E.A., Martin W., Esser C., Ahmadinejad N., Wiegand C., Madupu R.,
RA Beanan M.J., Brinkac L.M., Daugherty S.C., Durkin A.S., Kolonay J.F.,
RA Nelson W.C., Mohamoud Y., Lee P., Berry K.J., Young M.B., Utterback T.R.,
RA Weidman J.F., Nierman W.C., Paulsen I.T., Nelson K.E., Tettelin H.,
RA O'Neill S.L., Eisen J.A.;
RT "Phylogenomics of the reproductive parasite Wolbachia pipientis wMel: a
RT streamlined genome overrun by mobile genetic elements.";
RL PLoS Biol. 2:327-341(2004).
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 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=AAS14257.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AE017196; AAS14257.1; ALT_INIT; Genomic_DNA.
DR AlphaFoldDB; Q73HK8; -.
DR SMR; Q73HK8; -.
DR STRING; 163164.WD_0549; -.
DR EnsemblBacteria; AAS14257; AAS14257; WD_0549.
DR KEGG; wol:WD_0549; -.
DR eggNOG; COG0653; Bacteria.
DR OMA; MVHYDVQ; -.
DR Proteomes; UP000008215; 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; 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 membrane; Cytoplasm; Membrane; Metal-binding;
KW Nucleotide-binding; Protein transport; Translocase; Translocation;
KW Transport; Zinc.
FT CHAIN 1..868
FT /note="Protein translocase subunit SecA"
FT /id="PRO_0000321039"
FT BINDING 87
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
FT BINDING 105..109
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
FT BINDING 500
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
FT BINDING 849
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 860
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
FT BINDING 861
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
SQ SEQUENCE 868 AA; 99965 MW; 76EF2E35452F07B4 CRC64;
MSFFFIRKIF GSTNKKIIKS FRKIVQQINA LETEMQSLSD EELAGKTEEF KQELKNGKTL
NDLLVPAFAV VREASRRFLN MRHFDVQLIG GMVLHNGMIS EMKTGEGKTL VATLAAYLNS
LEGKGVHVVT VNDYLAKRDT EWMSKLYNSL GVSVAFITNN LTDEERKEAY SADIVYSTNN
ELAFDYLRDN MKFSQEDMVQ RGFHYGIVDE VDSILIDEAR TPLIISGPVE ENNQIYKHIN
KIVTKLVDSD YEVDEKGRTV FLTEDGISRV EELLRSYNLI PENSSLYDTD SMIMTHYIDQ
ALRAYKLFTA DKDYIVKDGK VVIIDEFTGR MMEGRRYSDG LHQALEAKEN LEIQHENQTL
ASVTFQNYFR MYNKLSGMTG TAATEAEEFR DIYRLNVVKI PTNVPVKRVD IDDEIYGTEK
EKFNAVLKFI EECYKRLQPV LVGTVSIENS EKLSALLQSH SLKHSVLNAR YHEQEAYIIA
QAGVPGSITI ATNMAGRGTD IQLGGNAEMI AKVELKKIKN ADEREKKYQE IVERVKKDKE
IAIKAGGLCV VGTERHESRR IDDQLRGRSG RQGDPGLSKF FLSLEDDLMR IFGSDRMRSF
LQKVGLKNNE AIHHPWINKA LEKAQKKVEA RNYDVRKSLL KFDDVINNQR KVIFKQRNNI
LGNEINDLLE VYSEVNESVV EGIIQSGYYE DYIENIVKEF HTRYGITLDK EDLAKFLNKQ
EALNYINDKI QEFFTEKEKY FNSQHTTDLW NTIVKQMMIM TLDHLWREHL SVLESLRQSI
SLRAMGQKDP LNEFKREAFL MFESMLEKWK ELTIHRLAHF KLADNQEIGN RLHSARNSRL
PKVSRNDKCP CNSGKKYKHC HGAVTVVS
