SECA_LEPIN
ID SECA_LEPIN Reviewed; 908 AA.
AC Q8F4S9;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 10-AUG-2010, sequence version 2.
DT 03-AUG-2022, entry version 107.
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=LA_1960;
OS Leptospira interrogans serogroup Icterohaemorrhagiae serovar Lai (strain
OS 56601).
OC Bacteria; Spirochaetes; Leptospirales; Leptospiraceae; Leptospira.
OX NCBI_TaxID=189518;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=56601;
RX PubMed=12712204; DOI=10.1038/nature01597;
RA Ren S.-X., Fu G., Jiang X.-G., Zeng R., Miao Y.-G., Xu H., Zhang Y.-X.,
RA Xiong H., Lu G., Lu L.-F., Jiang H.-Q., Jia J., Tu Y.-F., Jiang J.-X.,
RA Gu W.-Y., Zhang Y.-Q., Cai Z., Sheng H.-H., Yin H.-F., Zhang Y., Zhu G.-F.,
RA Wan M., Huang H.-L., Qian Z., Wang S.-Y., Ma W., Yao Z.-J., Shen Y.,
RA Qiang B.-Q., Xia Q.-C., Guo X.-K., Danchin A., Saint Girons I.,
RA Somerville R.L., Wen Y.-M., Shi M.-H., Chen Z., Xu J.-G., Zhao G.-P.;
RT "Unique physiological and pathogenic features of Leptospira interrogans
RT revealed by whole-genome sequencing.";
RL Nature 422:888-893(2003).
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; AE010300; AAN49159.2; -; Genomic_DNA.
DR RefSeq; NP_712141.2; NC_004342.2.
DR RefSeq; WP_000615621.1; NC_004342.2.
DR AlphaFoldDB; Q8F4S9; -.
DR SMR; Q8F4S9; -.
DR STRING; 189518.LA_1960; -.
DR EnsemblBacteria; AAN49159; AAN49159; LA_1960.
DR GeneID; 61141839; -.
DR KEGG; lil:LA_1960; -.
DR PATRIC; fig|189518.3.peg.1953; -.
DR HOGENOM; CLU_005314_3_0_12; -.
DR InParanoid; Q8F4S9; -.
DR Proteomes; UP000001408; Chromosome I.
DR GO; GO:0031522; C:cell envelope Sec protein transport complex; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0015462; F:ABC-type protein transporter activity; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IBA:GO_Central.
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 GO; GO:0043952; P:protein transport by the Sec complex; IBA:GO_Central.
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; Reference proteome; Translocase;
KW Translocation; Transport.
FT CHAIN 1..908
FT /note="Protein translocase subunit SecA"
FT /id="PRO_0000320843"
FT REGION 871..908
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 871..898
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 908 AA; 103284 MW; F698942A79AB7587 CRC64;
MIQNILRVVF GSKFERDLKK LIPIVRQINS LEESIKGMDD STLSSQTKKF KERIVQGESL
DSILPEAFAT VREVSLRTMG MRHFDVQMMG GIALHGGNIS EMKTGEGKTL TSTLAVYLNS
LAGNGVHVVT VNDYLAKRDA NWMKPIYDFL GISVGVIQHD MDHEQRKVAY AADITYGTNN
EFGFDYLRDN MVSHKDHKVQ RSHFFAIVDE VDSILIDEAR TPLIISGPSD EATDKYVRVN
KIIPKLSEGE DFEVDEKARN VLLTEKGVSH VEEILSIENL YAPENVDLVH HVHQALKAHK
IFRVDKDYVV QQGQVVIIDE FTGRPMEGRR YSDGLHQAIE AKENVTIAKE SQTLASITFQ
NYFRMYDKLA GMTGTADTEA EEFKKIYNLD VIVIPPNVSV QRKDSPDRVY RTEKEKFQAI
LTEIRELQSK KQPVLVGTIS IEKSEVLSKM LASAGIQHNV LNAKFHQKEA EIVANAGKPG
AVTIATNMAG RGTDIVLGGA QLYKENLETW KDEDEIVKQF KESILRQNLE YAESLMQKMD
SGTKQKRASE ILSSVKIWKK NHEEVLAAGG LHILGTERHE ARRIDNQLRG RSGRQGDPGS
SRFYLSLQDD LMRIFGSDRI SGLMKWANMP EGQEIESKMV SNAIARAQKR VEGHNFDIRK
HLLEYDDVMN RQRIVIYKMR NEVLENEDIS PLISGFIEET VENQIVTHCE GNNPSAWNLE
SLKEWSDGLD LNLQIDEVEF KKSKNPQLSL FEKVSSTAKL KYESKAEKIG KDIWKLLERN
IFLDILDHRW KEHLYSMDHL REGIWTVGYS ERNPLVEYKL QGFRMFDTAI ENLKNEIVNF
IFRVEVSENS KLPEEKKEYK KVGQEITGGF QEFSGGNLNR SQSNGSSVTV TTSSGGGTER
KTSRRRKR
