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SECA_TRIV2
ID   SECA_TRIV2              Reviewed;         930 AA.
AC   Q3MB92;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   25-OCT-2005, sequence version 1.
DT   03-AUG-2022, entry version 104.
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=Ava_2124;
OS   Trichormus variabilis (strain ATCC 29413 / PCC 7937) (Anabaena variabilis).
OC   Bacteria; Cyanobacteria; Nostocales; Nostocaceae; Trichormus.
OX   NCBI_TaxID=240292;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29413 / PCC 7937;
RX   PubMed=25197444; DOI=10.4056/sigs.3899418;
RA   Thiel T., Pratte B.S., Zhong J., Goodwin L., Copeland A., Lucas S., Han C.,
RA   Pitluck S., Land M.L., Kyrpides N.C., Woyke T.;
RT   "Complete genome sequence of Anabaena variabilis ATCC 29413.";
RL   Stand. Genomic Sci. 9:562-573(2014).
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   -!- FUNCTION: Probably participates in protein translocation into and
CC       across both the cytoplasmic and thylakoid membranes in cyanobacterial
CC       cells. {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 inner membrane {ECO:0000255|HAMAP-
CC       Rule:MF_01382}; Peripheral membrane protein {ECO:0000255|HAMAP-
CC       Rule:MF_01382}; Cytoplasmic side {ECO:0000255|HAMAP-Rule:MF_01382}.
CC       Cellular thylakoid 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}.
CC   -!- SIMILARITY: Belongs to the SecA family. {ECO:0000255|HAMAP-
CC       Rule:MF_01382}.
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DR   EMBL; CP000117; ABA21744.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q3MB92; -.
DR   SMR; Q3MB92; -.
DR   STRING; 240292.Ava_2124; -.
DR   EnsemblBacteria; ABA21744; ABA21744; Ava_2124.
DR   KEGG; ava:Ava_2124; -.
DR   eggNOG; COG0653; Bacteria.
DR   HOGENOM; CLU_005314_3_0_3; -.
DR   OMA; MVHYDVQ; -.
DR   Proteomes; UP000002533; Chromosome.
DR   GO; GO:0031676; C:plasma membrane-derived thylakoid 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 inner membrane; Cell membrane; Cytoplasm; Membrane;
KW   Nucleotide-binding; Protein transport; Thylakoid; Translocase;
KW   Translocation; Transport.
FT   CHAIN           1..930
FT                   /note="Protein translocase subunit SecA"
FT                   /id="PRO_0000318306"
FT   BINDING         83
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
FT   BINDING         101..105
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
FT   BINDING         491
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
SQ   SEQUENCE   930 AA;  106161 MW;  337B4BA5BD46FC4F CRC64;
     MLKLLLGDPN ARKLKKYQPY ITEINLLEED IKVLSDEDLK GKTAEFKQRL AKGETLDDIL
     PEAFAVVREA GRRVLGLRHF DVQMLGGVIL HSGQIAEMKT GEGKTLVATL PSYLNALTGK
     GVHVITVNDY LARRDAEWMG QVHRFLGLSV GLIQSSMTPS ERQKNYECDI TYVTNSEVGF
     DYLRDNMATS MADVVQRPFN YCVIDEVDSI LVDEARTPLI ISGQVERPTE KYVQAAEIAL
     TLQKDEHYEV DEKARNVLLT DEGFAQAEEL LGVTDLFDPE DPWAHFVFNA IKAKELFLKD
     VNYIVRNGEV VIVDEFTGRV LPGRRWSDGL HQAIEAKEHV DIQPETQTLA TITYQNLFLL
     YPKLGGMTGT AKTEEAEFER IYKLEVTIIP TNRIRRREDL SDLVFKKEIG KWQAIARECA
     EMHELGRPVL VGTTSVEKSE YLSQLLREQG IPHELLNARP ENVEREAEIV AQAGRRGAVT
     IATNMAGRGT DIILGGNSEY MARLKLREYF MPRIVRPDDE DVFGVQRAAG LPTGHGAGQG
     FVPGKKVKTW KASPEIFPTQ LSKEAEQLLK EAVDFAVREY GDRSLPELEA EDKVAVAAEK
     APTNDPVIQK LRDAYKRIKQ EYEEFTSTEH DEVVSRGGLH VIGTERHESR RIDNQLRGRA
     GRQGDPGSTR FFLSLEDNLL RIFGGDRVAG LMEAFNVEDD MPIESGMLTR SLEGAQRKVE
     TYYYDIRKQV FEYDEVMNNQ RRAIYAERRR VLEGQDLKEQ VIKYAEKTMD EIVDYYINVD
     LPSEEWELDK LVDKVKEFVY LLSDMQASQL EDMGVSEIKA FLHEQVRIAY DLKEAQIDQI
     QPGLMRQAER FFILQRIDTL WREHLQQMDA LRESVGLRGY GQKDPLIEYK SEGYELFLDM
     MVNIRRDVVY SLFMFQPQPQ PVVQTSSEMV
 
 
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