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SECA_THEYD
ID   SECA_THEYD              Reviewed;         880 AA.
AC   B5YKT5;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   25-NOV-2008, sequence version 1.
DT   03-AUG-2022, entry version 82.
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=THEYE_A1021;
OS   Thermodesulfovibrio yellowstonii (strain ATCC 51303 / DSM 11347 / YP87).
OC   Bacteria; Nitrospirae; Thermodesulfovibrionia; Thermodesulfovibrionales;
OC   Thermodesulfovibrionaceae; Thermodesulfovibrio.
OX   NCBI_TaxID=289376;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51303 / DSM 11347 / YP87;
RA   Dodson R.J., Durkin A.S., Wu M., Eisen J., Sutton G.;
RT   "The complete genome sequence of Thermodesulfovibrio yellowstonii strain
RT   ATCC 51303 / DSM 11347 / YP87.";
RL   Submitted (AUG-2008) to the EMBL/GenBank/DDBJ databases.
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   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01382};
CC       Note=May bind 1 zinc ion per subunit. {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       Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01382}. Note=Distribution is 50-
CC       50. {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; CP001147; ACI20371.1; -; Genomic_DNA.
DR   RefSeq; WP_012545108.1; NC_011296.1.
DR   RefSeq; YP_002248850.1; NC_011296.1.
DR   AlphaFoldDB; B5YKT5; -.
DR   SMR; B5YKT5; -.
DR   STRING; 289376.THEYE_A1021; -.
DR   EnsemblBacteria; ACI20371; ACI20371; THEYE_A1021.
DR   KEGG; tye:THEYE_A1021; -.
DR   PATRIC; fig|289376.4.peg.1002; -.
DR   eggNOG; COG0653; Bacteria.
DR   HOGENOM; CLU_005314_3_0_0; -.
DR   InParanoid; B5YKT5; -.
DR   OMA; MVHYDVQ; -.
DR   OrthoDB; 212453at2; -.
DR   Proteomes; UP000000718; Chromosome.
DR   GO; GO:0031522; C:cell envelope Sec protein transport complex; IBA:GO_Central.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR   GO; GO:0015462; F:ABC-type protein transporter activity; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IBA:GO_Central.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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   GO; GO:0043952; P:protein transport by the Sec complex; IBA:GO_Central.
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; IPR004027; SEC_C_motif.
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; PF02810; SEC-C; 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   Metal-binding; Nucleotide-binding; Protein transport; Reference proteome;
KW   Translocase; Translocation; Transport; Zinc.
FT   CHAIN           1..880
FT                   /note="Protein translocase subunit SecA"
FT                   /id="PRO_1000145073"
FT   REGION          837..871
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        837..860
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
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         511
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
FT   BINDING         864
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
FT   BINDING         866
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
FT   BINDING         875
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
FT   BINDING         876
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
SQ   SEQUENCE   880 AA;  101086 MW;  33D8229E90F2BB8A CRC64;
     MVKILEKIFG TKNERELKRY FTIVEDINRL ESQISSLSDE KLKQKTDEFR ERLAKGESLD
     DILKEAFAVV REVAKRTLGM RHFDVQLVGG LVLHEGKIAE MKTGEGKTLV ATLAAYLNAL
     EGKGVHIVTV NDYLARRDVQ WMGAIYNFLG LSVGVIQPDA SFLYDPNYRL PDRRFDRLRP
     CSKKEAYLAD ITYGTNNEFG FDYLRDNMRY SIDELCQREL NYAIVDEVDS ILIDEARTPL
     IISGPSEEST DIYYAVNRII KYLKPENDFK LDEKLKTVVL TEQGSQKAEK LLGIDNLYNP
     SNIQVVHHIN QAIRAHYFFK KEVDYVVKDG KIVIVDEFTG RLLEGRRWSD GLHQAIEAKE
     GLKIEAENQT LATITFQNYF RMYKKLAGMT GTADTEASEF AEIYNLEVVV IPTHKPMIRE
     DYPDAVYKTE KAKYEAVVKE IEECYKVGRP VLVGTTSIEK SELISKMLKK KGVPHNVLNA
     KYHDKEAEIV AQAGRIGAVT IATNMAGRGT DILLGGNPEF LAREMLAGKD YTEEEYKKAL
     EKAKEICKEE HDKVVSLGGL HIIGTERHES RRIDNQLRGR AGRQGDPGSS RFYLSLEDEL
     LRLFGGERLQ SLMHFLKIED DTPIENKMVS KAIENAQKRV EAHNFDIRKH LLKYDDVMNS
     QRNEIYSFRK EVLESDSLKD KVFELLEIEI DEMVDFYLAQ ESEGVEKLKE QLSARFDIEV
     DLSNKSKDEI KEYLLEKLRE AYEKKEQKIG QELMRDVEKM IFLHVIDTKW KDHLLGIDHI
     KEGIGLRGYA QRDPLVEYKK EAFELFEEMS RNIISDILTR LFKIQIKEES QVKVARAQKI
     QRSDGDGARR PVEKPKKIGR NDPCPCGSGK KYKKCCGKNS
 
 
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