SECA_LEPBA
ID SECA_LEPBA Reviewed; 918 AA.
AC B0SEW5;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 08-APR-2008, sequence version 1.
DT 03-AUG-2022, entry version 87.
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=LBF_2759;
OS Leptospira biflexa serovar Patoc (strain Patoc 1 / Ames).
OC Bacteria; Spirochaetes; Leptospirales; Leptospiraceae; Leptospira.
OX NCBI_TaxID=355278;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Patoc 1 / Ames;
RX PubMed=18270594; DOI=10.1371/journal.pone.0001607;
RA Picardeau M., Bulach D.M., Bouchier C., Zuerner R.L., Zidane N.,
RA Wilson P.J., Creno S., Kuczek E.S., Bommezzadri S., Davis J.C., McGrath A.,
RA Johnson M.J., Boursaux-Eude C., Seemann T., Rouy Z., Coppel R.L.,
RA Rood J.I., Lajus A., Davies J.K., Medigue C., Adler B.;
RT "Genome sequence of the saprophyte Leptospira biflexa provides insights
RT into the evolution of Leptospira and the pathogenesis of leptospirosis.";
RL PLoS ONE 3:E1607-E1607(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 -!- 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; CP000777; ABZ95239.1; -; Genomic_DNA.
DR RefSeq; WP_012389786.1; NC_010842.1.
DR AlphaFoldDB; B0SEW5; -.
DR SMR; B0SEW5; -.
DR PRIDE; B0SEW5; -.
DR KEGG; lbf:LBF_2759; -.
DR HOGENOM; CLU_005314_3_0_12; -.
DR OMA; MVHYDVQ; -.
DR BioCyc; LBIF355278:LBF_RS14030-MON; -.
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..918
FT /note="Protein translocase subunit SecA"
FT /id="PRO_1000184235"
FT REGION 863..918
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 863..889
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 891..909
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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 494
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
SQ SEQUENCE 918 AA; 105350 MW; 0A2FC6530E353770 CRC64;
MFQKILTILF GSKYERDLKR LNPIVETINS FEVTIKAMDD ETLSSQTKKF KERLASGETL
DDILPEAFAT VREVAYRTLG MRHFDVQMMG GISLHWGNIS EMKTGEGKTL TSTLPIYLNS
LSGEGVHVVT VNDYLAKRDA NWMRPVFEFL KVSVGVIQHD MDHEERKVAY NSDITYGTNN
EFGFDYLRDN MVSYKEHRVQ RQHNFAIVDE VDSILIDEAR TPLIISGPAE ESTDKYLKVN
KIIPKLVEGE DFEIDEKAKN VILSEAGVHH VEKLLEVDNL YHAENIELVH HVQQALKAHK
IFFKDKDYVV QDGEVIIVDE FTGRLMKGRR YSDGLHQSLE AKEGVPIARE SQTLASITFQ
NYFRIYKKLA GMTGTADTEA EEFKKIYNLD VIVIPSNLKI QRQDMPDRVY KTEREKFDAV
VKDIQEKVSR KQPVLVGTIS IEKSEVLSKL LFSHGIQHNV LNAKQHERES EIVANAGKPG
AITIATNMAG RGTDIVLGGA PKYKDDLEKL DDKCDSLGIK NKEELEIIYS FRECLIKQKF
DEAEGKISDV RNETIKKECI KILGDAKKWK VDHDFVIGAG GLHIIGSERH ESRRIDNQLR
GRSGRQGDPG SSRFYLSLQD DLMRIFGSDR IARIMDTLKM PEGQELEHSM VSNAIARAQK
RVEGHNFDIR KHLLEYDDVM NRQRIYIYGI RNELLDKGNM SKTVFDFFDE VVENQVILYC
EGNNADAWEI DSLNEWLQSL GIDHKIESKD FKKESNPQLK VFEVVSKLVK ELYDYKVSSI
GDEIWRSIER NVFLDILDHR WKEHLYAMDH LKEGIWTVGY GEKNPLIEYK LQGFKMFDQL
VDNLKNEVVS FLLKIEVTES DKKQDDTSPK EYKKIGQEQR AEVDMFGNEL KSNKTKPQVS
STTSSGGGSE RRSSRRKK
