SECA2_CORJK
ID SECA2_CORJK Reviewed; 771 AA.
AC Q4JVU1;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 02-AUG-2005, sequence version 1.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=Protein translocase subunit SecA 2 {ECO:0000255|HAMAP-Rule:MF_01382};
DE EC=7.4.2.8 {ECO:0000255|HAMAP-Rule:MF_01382};
GN Name=secA2 {ECO:0000255|HAMAP-Rule:MF_01382}; OrderedLocusNames=jk0902;
OS Corynebacterium jeikeium (strain K411).
OC Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae;
OC Corynebacterium.
OX NCBI_TaxID=306537;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K411;
RX PubMed=15968079; DOI=10.1128/jb.187.13.4671-4682.2005;
RA Tauch A., Kaiser O., Hain T., Goesmann A., Weisshaar B., Albersmeier A.,
RA Bekel T., Bischoff N., Brune I., Chakraborty T., Kalinowski J., Meyer F.,
RA Rupp O., Schneiker S., Viehoever P., Puehler A.;
RT "Complete genome sequence and analysis of the multiresistant nosocomial
RT pathogen Corynebacterium jeikeium K411, a lipid-requiring bacterium of the
RT human skin flora.";
RL J. Bacteriol. 187:4671-4682(2005).
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; CR931997; CAI37066.1; -; Genomic_DNA.
DR RefSeq; WP_011273492.1; NC_007164.1.
DR AlphaFoldDB; Q4JVU1; -.
DR SMR; Q4JVU1; -.
DR STRING; 306537.jk0902; -.
DR EnsemblBacteria; CAI37066; CAI37066; jk0902.
DR KEGG; cjk:jk0902; -.
DR PATRIC; fig|306537.10.peg.914; -.
DR eggNOG; COG0653; Bacteria.
DR HOGENOM; CLU_005314_3_2_11; -.
DR OMA; WADHLAF; -.
DR OrthoDB; 212453at2; -.
DR Proteomes; UP000000545; 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; -; 3.
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; IPR026389; SecA_Actinobact_type.
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; TIGR04221; SecA2_Mycobac; 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..771
FT /note="Protein translocase subunit SecA 2"
FT /id="PRO_0000318346"
FT BINDING 91
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
FT BINDING 109..113
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 771 AA; 84553 MW; D5FBC2EA70B9CC4A CRC64;
MAFDWFWKAM GSSPKKNQKK SRAVVAQADS SRYSGLSDAE LRDAASDVVT EQSTSEDGHH
FGGQVDDAPA LLAILREAAS RTLNMEPFDV QMQGTYRLLH GDVVEMATGE GKTLAGAMAA
VGFALQGKRV HVITVNSYLA GRDNDWMGPM FDFFGLTHGA IREDLTADQR RDIYSRDVIF
GAINELGFDV LRDQLITRRA DQVRTPADVA VIDEADSVMV DEALVPLVLA GSEPGPAPAG
RITDLVKRME EDKHFHVSED HRNVFLTDEG AAFVEKELGV DSLYEDEGEL LVQVNVALHA
EHLLIRDVHY IVRDGKVALI DGSRGRVAEL QRWPDGLQAA VEAKEGLDVT DGGRILDQIT
IQALVGMYPE VCGMTGTALA AGDQLRQFYN LQVSVIEPNV PNIRFDEADR VYVSAAERND
AVVKHIVEVQ KTGQPQLVGT QDVAESEELA EALLSAGVEC SVLNAKNHEA EAAVVAEAGR
PGRVTVSTQM AGRGTDIKLG GTDEAEHDEV VETGGLHVVG VGRFRSQRLD NQLRGRAGRQ
GDPGSSLFFV SLEDDVVAVG GAGEELQAQP EEDGLLPQKK VQQFVDHCQR VTEGQMLDIH
ATTWKYNKLI KDQRDIVNDR RDTLLDTAAA WDDLSYHNVD RAAELKKQGI SEEVLEQAAR
EIMLFHLDNE WSEHLAYLDD VRESIHLRAI ARESPIDEFH RMSIAAFGEL AERAVNKARE
TFDEVEITSD GAQLGEMGLH KPSATWTYMV NDNPLSSSGG SVMGSIVQMF R
