SECA_BORBU
ID SECA_BORBU Reviewed; 899 AA.
AC O07497; O51176;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-1998, sequence version 2.
DT 03-AUG-2022, entry version 137.
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=BB_0154;
OS Borreliella burgdorferi (strain ATCC 35210 / DSM 4680 / CIP 102532 / B31)
OS (Borrelia burgdorferi).
OC Bacteria; Spirochaetes; Spirochaetales; Borreliaceae; Borreliella.
OX NCBI_TaxID=224326;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Sh-2;
RX PubMed=9565653; DOI=10.1016/s0005-2736(97)00277-0;
RA Guina T., Helfet-Hilliker D., Ramamurthy V., Oliver D.;
RT "Sequence and phylogenetic analysis of the Borrelia burgdorferi secA
RT gene.";
RL Biochim. Biophys. Acta 1371:24-30(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35210 / DSM 4680 / CIP 102532 / B31;
RX PubMed=9403685; DOI=10.1038/37551;
RA Fraser C.M., Casjens S., Huang W.M., Sutton G.G., Clayton R.A.,
RA Lathigra R., White O., Ketchum K.A., Dodson R.J., Hickey E.K., Gwinn M.L.,
RA Dougherty B.A., Tomb J.-F., Fleischmann R.D., Richardson D.L.,
RA Peterson J.D., Kerlavage A.R., Quackenbush J., Salzberg S.L., Hanson M.,
RA van Vugt R., Palmer N., Adams M.D., Gocayne J.D., Weidman J.F.,
RA Utterback T.R., Watthey L., McDonald L.A., Artiach P., Bowman C.,
RA Garland S.A., Fujii C., Cotton M.D., Horst K., Roberts K.M., Hatch B.,
RA Smith H.O., Venter J.C.;
RT "Genomic sequence of a Lyme disease spirochaete, Borrelia burgdorferi.";
RL Nature 390:580-586(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 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. Other proteins may also be involved.
CC {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; AF003354; AAC46347.1; -; Genomic_DNA.
DR EMBL; AE000783; AAC66536.1; -; Genomic_DNA.
DR PIR; B70119; B70119.
DR RefSeq; NP_212288.1; NC_001318.1.
DR RefSeq; WP_002665461.1; NC_001318.1.
DR AlphaFoldDB; O07497; -.
DR SMR; O07497; -.
DR STRING; 224326.BB_0154; -.
DR PRIDE; O07497; -.
DR EnsemblBacteria; AAC66536; AAC66536; BB_0154.
DR KEGG; bbu:BB_0154; -.
DR PATRIC; fig|224326.49.peg.551; -.
DR HOGENOM; CLU_005314_3_0_12; -.
DR OMA; MVHYDVQ; -.
DR Proteomes; UP000001807; 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..899
FT /note="Protein translocase subunit SecA"
FT /id="PRO_0000109577"
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 516
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
FT BINDING 884
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
FT BINDING 886
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
FT BINDING 895
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
FT BINDING 896
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
FT CONFLICT 265
FT /note="L -> F (in Ref. 1; AAC46347)"
FT /evidence="ECO:0000305"
FT CONFLICT 406
FT /note="H -> D (in Ref. 1; AAC46347)"
FT /evidence="ECO:0000305"
FT CONFLICT 475
FT /note="N -> S (in Ref. 1; AAC46347)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 899 AA; 102086 MW; 40B2221217B870AA CRC64;
MLKAVLETTI GSKSKRDLKD YLPTLRNINK LERWALLLAD EDFSKETEKL KDELKSGNSL
ENILERAFTL SREAARRRLK ERPYDVQIIA GLALHKGKII EMKTGEGKTL SSVQAAYLNS
LTGDGVIIVT VNDYLAERDS NWMKPVFDLL GVSVGVVLSN MDYELRKAQY AKDITYVTNN
ELGFDYLRDN MRYDLNEKSL RKFNYCIIDE IDSILIDEAR TPLIISGPTE GNTNAYLEVN
SLVSFLKECS KDPKTGDYPL EIDDLDGDYT VDEKAKRISF TAKGLNNLEQ LLVSKGIISG
SMYTDSNFNY VHYMTQALKA HLLFLKNREY IVGDSGVEIV DEFTGRVLTG RRYSDGLHQA
IEAKEGVRVA NENKTMATIT FQNLFRMFDK ISGMTGTADT EAKEFHKIYN LDVVVVPTNR
LLARIDEDDT IYYTEEFKFN AITDEVYKTY KKGQPVLVGT VSIEKSEILS AMFKNRGIKH
EVLNAKNHSR EAFIIAEAGA KHAVTIATNM AGRGTDIKLG GNIEHRVRKK IGTNVSLEEF
QEAVKNEREN YLKDYNEVKS LGGLYVIGSE RHESRRIDNQ LRGRSGRQGD PGRSRFYVSL
EDDLMRLFAG DNLRSLMGKL GMATGEPITH SLLTKSLINA QKRVEDRNFE IRKHLLEYDD
VITKQRDFIY AQRNSILEDT AIKDRILVAL EEYLSFLLEG TKSSTVSNVF LNEVNSIFAY
MLESLGSIEN ISSLDLKAKL MQIAKANLDE KENLIGRDLF NGFLRYEYLK NIDFKFQEHL
ANLDSLREAV YLRSYANKNP ITEYKEEGFS IFSELIKDIK VSTIRRVLQL KLDSNSSDFK
STKKSRNVKP IHKELSGIVI NENKSASNVQ VVRSSPKIGR NEPCYCGSGK KYKNCHGKS
