SECA_LIGS1
ID SECA_LIGS1 Reviewed; 787 AA.
AC Q1WSW8;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 02-MAY-2006, sequence version 1.
DT 03-AUG-2022, entry version 103.
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=LSL_1186;
OS Ligilactobacillus salivarius (strain UCC118) (Lactobacillus salivarius).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC Ligilactobacillus.
OX NCBI_TaxID=362948;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UCC118;
RX PubMed=16617113; DOI=10.1073/pnas.0511060103;
RA Claesson M.J., Li Y., Leahy S., Canchaya C., van Pijkeren J.P.,
RA Cerdeno-Tarraga A.M., Parkhill J., Flynn S., O'Sullivan G.C., Collins J.K.,
RA Higgins D., Shanahan F., Fitzgerald G.F., van Sinderen D., O'Toole P.W.;
RT "Multireplicon genome architecture of Lactobacillus salivarius.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:6718-6723(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 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}.
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DR EMBL; CP000233; ABD99994.1; -; Genomic_DNA.
DR RefSeq; WP_003700639.1; NC_007929.1.
DR RefSeq; YP_536077.1; NC_007929.1.
DR AlphaFoldDB; Q1WSW8; -.
DR SMR; Q1WSW8; -.
DR STRING; 362948.LSL_1186; -.
DR EnsemblBacteria; ABD99994; ABD99994; LSL_1186.
DR GeneID; 57059616; -.
DR KEGG; lsl:LSL_1186; -.
DR PATRIC; fig|362948.14.peg.1261; -.
DR HOGENOM; CLU_005314_3_2_9; -.
DR OMA; MVHYDVQ; -.
DR Proteomes; UP000006559; 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: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; 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 membrane; Cytoplasm; Membrane; Nucleotide-binding;
KW Protein transport; Reference proteome; Translocase; Translocation;
KW Transport.
FT CHAIN 1..787
FT /note="Protein translocase subunit SecA"
FT /id="PRO_1000073485"
FT BINDING 85
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
FT BINDING 103..107
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
FT BINDING 492
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
SQ SEQUENCE 787 AA; 89834 MW; 7E8A69FCCD26242E CRC64;
MANLLKRWVE SDKRELKRLG KIADKVESYA DEFGALSDDE LKAKTEEFKK RYQDGESLDD
LLPEAFAVCR EGAKRVLGLY PYHVQIIGGI VLHEGNIAEM KTGEGKTLTA TMPVYLNAIS
GKGVHVVTVN EYLSERDATE MGELYTWLGL TVGLNLADKS PEEKRNAYNC DITYSTNSEL
GFDYLRDNMV VYKEDMVQRP LNFVIVDEVD SILIDEARTP LIISGQATGT TTLYTRTDRF
AKTLTEDEDF KIDLESKTVS LTEDGIRKGE KYFGLKNLYD PDNMALNHHL DNALRANYIM
LRDKDYVVRD GEVLIVDQFT GRIMDGRRYS DGLHQAIEAK EHVEIEEETK TMANITYQNF
FRMYNKLSGM TGTAKTEREE FREIYNMEVV SIPTNKPIAR VDKPDLLYPT LKSKFNAVVR
DVKARHEKGQ PVLVGTVAVE TSELLSKMLD DEGIPHSVLN AKNHAREAEI VMNAGQRGAV
TIATNMAGRG TDIKLGPGVR ELGGLAVIGT ERHESRRIDN QLRGRSGRQG DPGVTQFYLS
LEDDLMLRFG SERIKNFLER MKVSDDDAVI QSKMISRQVE SAQKRVEGNN YDTRKQVLQY
DDVMRAQREV IYAQRQQVIM EEKSLKPIIM PMIERTVKHT VLMHTQGDKS EWNLQGILDF
AVSAMVNEDT ISLGDLVNKT PDEIVDYLMK RAEDIYAEKE KQLYDESQML EFEKVVILRV
VDSLWTDHID EMDQLRQSIG LRGYGQLNPL VEYQQDGFRM FEQMVGAIEY DVTRLFLKAE
IRQDIKR
