SECA1_CORJK
ID SECA1_CORJK Reviewed; 867 AA.
AC Q4JTQ3;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 02-AUG-2005, sequence version 1.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=Protein translocase subunit SecA 1 {ECO:0000255|HAMAP-Rule:MF_01382};
DE EC=7.4.2.8 {ECO:0000255|HAMAP-Rule:MF_01382};
GN Name=secA1 {ECO:0000255|HAMAP-Rule:MF_01382}; OrderedLocusNames=jk1630;
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; CAI37804.1; -; Genomic_DNA.
DR RefSeq; WP_011274016.1; NC_007164.1.
DR AlphaFoldDB; Q4JTQ3; -.
DR SMR; Q4JTQ3; -.
DR STRING; 306537.jk1630; -.
DR EnsemblBacteria; CAI37804; CAI37804; jk1630.
DR KEGG; cjk:jk1630; -.
DR PATRIC; fig|306537.10.peg.1649; -.
DR eggNOG; COG0653; Bacteria.
DR HOGENOM; CLU_005314_3_2_11; -.
DR OMA; MVHYDVQ; -.
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; -; 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 membrane; Cytoplasm; Membrane; Nucleotide-binding;
KW Protein transport; Reference proteome; Translocase; Translocation;
KW Transport.
FT CHAIN 1..867
FT /note="Protein translocase subunit SecA 1"
FT /id="PRO_0000318345"
FT BINDING 86
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
FT BINDING 104..108
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
FT BINDING 493
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
SQ SEQUENCE 867 AA; 98001 MW; 1C0E4315C53126B7 CRC64;
MLGLSKILRM GEGRAVKRLA KIADQVMDLD EEYTKLTDEE LQAKTDELKK RVQEDGESLD
DILLEAFATA REASWRVLGQ KHYKVQIMGG AGLHFGYVSE MKTGEGKTLT CVLPAYLNAL
SGKGVHVVTV NDYLAKRDAE WMGRVHRFLG LSTDVILSGK NPAERREAYN ADITYGTNNE
FGFDYLRDNM AHSLNDLVQR GHNYAIVDEV DSILIDEART PLIISGPVEG SSKWFSAFAA
IAPKLTRDIH YEVDERKKTV GVKEEGVEFV EDQLGIENLY APEHSQLVSY LNNSIKAKEL
FTRDKDYIVR NGEVVIVDEF TGRILDGRRY NEGIHQAIEA KEHVEIKNEN QTLATVTLQN
YFRLYDKLAG MTGTAETEAA ELKSTYKLDV AAIPTNKENK RKDNVDLIYK TQEAKFEAVA
EDIAERVEIG QPVLVGTTSV ERSEYLSRLL QRRGIKHNVL NAKYHEKEAE IVAQAGRLGA
VTVATNMAGR GTDIVLGGNP DIIADINLRE RGLDPVETPE EYEEAWDDEI EKVRKESKEE
AEKVREVGGL YVLGTERHES RRIDNQLRGR SARQGDPGET RFYLSMRDDL MVRFVGQTME
AMMTRLNIPD DEAIDSKMVT NAIKGAQSQV ESANFEMRKN VLKYDEVMNE QRKVIYGERR
QILEGEDVEK QIRSMLKDTI EAYVDGATAE GYVEDWDLDT LWNALDSLYG PTFTHEELVE
GDEYGRPGEL SSSQLLDALL EDANREYDEL EEKVSEVAGE EQMRGMERAA LLNVVDQKWR
EHLYEMDYLK EGIGLRAMAQ RDPLVEYQRE GGDMFNRMKD GIKEETVRQL FLVRNQLKQA
GQVHVEDPAA GNEGVAVDRA TQTTMGG
