SECA_LEUCK
ID SECA_LEUCK Reviewed; 804 AA.
AC B1MW27;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 29-APR-2008, sequence version 1.
DT 03-AUG-2022, entry version 91.
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=LCK_01608;
OS Leuconostoc citreum (strain KM20).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC Leuconostoc.
OX NCBI_TaxID=349519;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KM20;
RX PubMed=18281406; DOI=10.1128/jb.01862-07;
RA Kim J.F., Jeong H., Lee J.-S., Choi S.-H., Ha M., Hur C.-G., Kim J.-S.,
RA Lee S., Park H.-S., Park Y.-H., Oh T.K.;
RT "Complete genome sequence of Leuconostoc citreum KM20.";
RL J. Bacteriol. 190:3093-3094(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 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; DQ489736; ACA83431.1; -; Genomic_DNA.
DR RefSeq; WP_012305437.1; NC_010471.1.
DR AlphaFoldDB; B1MW27; -.
DR SMR; B1MW27; -.
DR STRING; 349519.LCK_01608; -.
DR EnsemblBacteria; ACA83431; ACA83431; LCK_01608.
DR KEGG; lci:LCK_01608; -.
DR eggNOG; COG0653; Bacteria.
DR HOGENOM; CLU_005314_3_0_9; -.
DR OMA; MVHYDVQ; -.
DR OrthoDB; 212453at2; -.
DR Proteomes; UP000002166; 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; Translocase; Translocation; Transport.
FT CHAIN 1..804
FT /note="Protein translocase subunit SecA"
FT /id="PRO_1000145031"
FT BINDING 100
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
FT BINDING 118..122
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
FT BINDING 508
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
SQ SEQUENCE 804 AA; 90737 MW; 8EB88556D741A94C CRC64;
MANPIRKLVD NSKKQLKKLN HIADKVEDYA DEMAALSDEA LQAKTPVFKE KIADALRDVT
ETDKQNKVLA KTLDALLPEA FAVAREAAKR VLGLYPFRVQ IMGAAVLNDG NLAEMRTGEG
KTLTATMAVY LNALTDRGVH VVTVNDYLSA RDAEQMGQLY NWLGLSVGVN VGDAPAEEKR
AAYDADITYS TNFNIGFDYL RDNMVRRAEE RVMQRGLNFA LIDEADSILI DTARTPLIIS
GPGSGVSQLY GRADRFVKTL QQDEDYKIDE EAKTTMLTND GIHKGEIFFN LDNLYDAGDT
ALTHHIDQAL RANFNYINDK DYVVQDGEVK LIDQSTGRIS EGTRLSDGLH QAIEAKEGVE
IQEENKSMAQ ITYQNLFRMY KKLSGMTGTA KTEEEELREI YNMEVITIPT NRPIKRVDYP
DLLYPSIRAK YNAVVKLIQE LHEKGQPILI GTGSVESSEL LSKILMAQNV PHNVLNAKNN
AKEAEIIANA GQRGAVTVAT NMAGRGTDIK LGPGVADLGG LAVIATERHE SRRIDNQLRG
RAGRQGDDGF SQFFLSLEDD LMIRFGAERI RAVWERMNLD EEETVIKNRL ITRSVESAQK
RVEGNNYDTR KNVLQYDDVV REQRELIYHQ RDIIIDESQS LDWVLMPMVS RTINRVVTVQ
TKSKKPSEWQ LQQIIVFAEN VLVNEGALTE NDLSGLSRED IEAKLYALAK ENYANKKRQL
YEPEQMLEFE KVVILRAVDQ HWTDHIDALD RLRQGVGLRG YGQLNPLIEY QNEAFENFNK
MIADVEYDAT RTFMKAEIRQ NLKA
