SECA_LEPBJ
ID SECA_LEPBJ Reviewed; 904 AA.
AC Q04SJ8;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 14-NOV-2006, sequence version 1.
DT 03-AUG-2022, entry version 92.
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=LBJ_1552;
OS Leptospira borgpetersenii serovar Hardjo-bovis (strain JB197).
OC Bacteria; Spirochaetes; Leptospirales; Leptospiraceae; Leptospira.
OX NCBI_TaxID=355277;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JB197;
RX PubMed=16973745; DOI=10.1073/pnas.0603979103;
RA Bulach D.M., Zuerner R.L., Wilson P., Seemann T., McGrath A., Cullen P.A.,
RA Davis J., Johnson M., Kuczek E., Alt D.P., Peterson-Burch B., Coppel R.L.,
RA Rood J.I., Davies J.K., Adler B.;
RT "Genome reduction in Leptospira borgpetersenii reflects limited
RT transmission potential.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:14560-14565(2006).
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 -!- 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; CP000350; ABJ76122.1; -; Genomic_DNA.
DR AlphaFoldDB; Q04SJ8; -.
DR SMR; Q04SJ8; -.
DR EnsemblBacteria; ABJ76122; ABJ76122; LBJ_1552.
DR KEGG; lbj:LBJ_1552; -.
DR HOGENOM; CLU_005314_3_0_12; -.
DR OMA; MVHYDVQ; -.
DR Proteomes; UP000000656; Chromosome 1.
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: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; 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; 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 Nucleotide-binding; Protein transport; Translocase; Translocation;
KW Transport.
FT CHAIN 1..904
FT /note="Protein translocase subunit SecA"
FT /id="PRO_1000073487"
FT REGION 870..904
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 870..894
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 89
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
FT BINDING 107..111
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
FT BINDING 496
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
SQ SEQUENCE 904 AA; 103100 MW; F5A429DB8AD406FD CRC64;
MNMIQNILRV ILGSKFERDL KKLVPIVGQI NSLEKEMKET SDSLLSSQTQ KFRERIARGE
SLDSILPEAF ATVREVSLRT MGMRHFDVQM MGGIALHRGN IAEMKTGEGK TLTSTLAVYL
NSLAGKGVHV VTVNDYLAKR DANWMKPIYD FLGISVGVIQ HDMDHEQRKI AYSADITYGT
NNEFGFDYLR DNMVSHKDHK VQRSHFFAIV DEVDSILIDE ARTPLIISGS SDETTDKYVR
INKIIPKLVA IEDFEVDEKA RNVLLSEKGV SHVEEILGIE NLYAPENVDL VHHVHQALKA
HKIFQKDVDY VVQNGEVIIV DEFTGRLMAG RRYSDGLHQA LEAKESVTIA KESQTLASIT
FQNYFRMYDK LAGMTGTADT EAEEFRKIYD LDVIVIPPNV SVRRKDSPDR VYRTEKEKFD
AILAEIRELQ SKKQPVLVGT ISIEKSEILS KMLSSAGIQH NVLNAKFHER EAEIVANAGK
PGAVTIATNM AGRGTDIVLG GAQLYKENLE TWKDDDDLVR RFKESILKQE LDNAELLIRE
MDSSVKQKRA SEILESVKIW KKNHEDVLVA GGLHILGTER HEARRIDNQL RGRSGRQGDP
GSSRFYLSLQ DDLMRIFGSD RISGLMKWAN MPEGQEIESK MVSNAIARAQ KRVEGHNFDI
RKHLLEYDDV MNRQRIVIYK MRNEVLENED ISSLILSFIE EAVENQIVAH CEGNNPSSWN
LDSLKEWLEG LELNLEINEE DFKKTKNPQL ALFEKVNAAA KQKYEDRAES IGKDIWKLLE
RNIFLDILDH RWKEHLYSMD HLREGIWTVG YSERNPLVEY KLQGFRMFDV AIENLKNEVV
NFLFRVEVSE NSKLPEERRE YKKVGQEVTG GFQELSSGTP SPTVTVTTSS GGGTERKTSR
RRKR
