SECA1_CORGB
ID SECA1_CORGB Reviewed; 845 AA.
AC A4QC94;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 15-MAY-2007, sequence version 1.
DT 03-AUG-2022, entry version 89.
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=cgR_0868;
OS Corynebacterium glutamicum (strain R).
OC Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae;
OC Corynebacterium.
OX NCBI_TaxID=340322;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=R;
RX PubMed=17379713; DOI=10.1099/mic.0.2006/003657-0;
RA Yukawa H., Omumasaba C.A., Nonaka H., Kos P., Okai N., Suzuki N., Suda M.,
RA Tsuge Y., Watanabe J., Ikeda Y., Vertes A.A., Inui M.;
RT "Comparative analysis of the Corynebacterium glutamicum group and complete
RT genome sequence of strain R.";
RL Microbiology 153:1042-1058(2007).
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; AP009044; BAF53841.1; -; Genomic_DNA.
DR RefSeq; WP_011896902.1; NC_009342.1.
DR AlphaFoldDB; A4QC94; -.
DR SMR; A4QC94; -.
DR EnsemblBacteria; BAF53841; BAF53841; cgR_0868.
DR KEGG; cgt:cgR_0868; -.
DR HOGENOM; CLU_005314_3_2_11; -.
DR OMA; MVHYDVQ; -.
DR PhylomeDB; A4QC94; -.
DR Proteomes; UP000006698; 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..845
FT /note="Protein translocase subunit SecA 1"
FT /id="PRO_0000318343"
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 845 AA; 95451 MW; 48366E1B93FEEC68 CRC64;
MFGLSKVLRV GEGRAVKRLH KIADQVIALE EKFANLTDEE LKAKTAEFKE RIAGGEGLDE
IFLEAFATAR EASWRVLGQK HYRVQIMGGA ALHFGNVAEM RTGEGKTLTC VLPAYLNALE
GKGVHVVTVN DYLAKRDAEM VGRVHRYLGL EVGVILSDMR PDERRKAYTA DITYGTNNEL
GFDYLRDNMA RSLSDLVQRG HNYAIVDEVD SILIDEARTP LIISGPVDGT SQFYNVFAQI
VPRMTKDVHY EVDERKKTVG VKEEGVEYVE DQLGIDNLYA PEHSQLVSYL NNAIKAQELF
TRDKDYIVRN GEVMIVDGFT GRVLAGRRYN EGMHQAIEAK ERVEIKNENQ TLATVTLQNY
FRLYTKLAGM TGTAETEAAE LNQIYKLDVI AIPTNRPNQR EDLTDLVYKT QEAKFAAVVD
DIAERTEKGQ PVLVGTVSVE RSEYLSQLLT KRGIKHNVLN AKHHEQEAQI VAQAGLPGAV
TVATNMAGRG TDIVLGGNPE ILLDIKLRER GLDPFEDEES YQEAWDAELP AMKQRCEERG
DKVREAGGLY VLGTERHESR RIDNQLRGRS ARQGDPGSTR FYLSMRDDLM VRFVGPTMEN
MMNRLNVPDD VPIESKTVTN SIKGAQAQVE NQNFEMRKNV LKYDEVMNEQ RKVIYSERRE
ILESADISRY IQNMIEETVS AYVDGATANG YVEDWDLDKL WNALEALYDP SINWTDLVEG
SEYGKPGELS AEDLRTALVN DAHAEYAKLE EAVSAIGGEA QIRNIERMVL MPVIDTKWRE
HLYEMDYLKE GIGLRAMAQR DPLVEYQKEG GDMFNGMKDG IKEETVRQLF LLRKQFIKQD
AEVAD
