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ZRAR_SALTY
ID   ZRAR_SALTY              Reviewed;         441 AA.
AC   P25852; Q9L9H8;
DT   01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2002, sequence version 2.
DT   03-AUG-2022, entry version 165.
DE   RecName: Full=Transcriptional regulatory protein ZraR;
GN   Name=zraR; Synonyms=hydG; OrderedLocusNames=STM4174; ORFNames=STMF1.27;
OS   Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=99287;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=1756170; DOI=10.1016/0167-4781(91)90224-a;
RA   Chopra A.K., Peterson J.W., Prasad R.;
RT   "Cloning and sequence analysis of hydrogenase regulatory genes (hydHG) from
RT   Salmonella typhimurium.";
RL   Biochim. Biophys. Acta 1129:115-118(1991).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX   PubMed=11677609; DOI=10.1038/35101614;
RA   McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA   Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA   Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA   Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA   Wilson R.K.;
RT   "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL   Nature 413:852-856(2001).
CC   -!- FUNCTION: Member of the two-component regulatory system ZraS/ZraR. When
CC       activated by ZraS it acts in conjunction with sigma-54 to regulate the
CC       expression of zraP. Positively autoregulates the expression of the
CC       zraSR operon (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC   -!- PTM: Phosphorylated by ZraS. {ECO:0000250}.
CC   -!- CAUTION: Was originally thought to be involved in the regulation of the
CC       labile hydrogenase activity. {ECO:0000305|PubMed:1756170}.
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DR   EMBL; M64988; AAA27149.1; -; mRNA.
DR   EMBL; AF170176; AAF33506.1; -; Genomic_DNA.
DR   EMBL; AE006468; AAL23002.1; -; Genomic_DNA.
DR   PIR; S19606; S19606.
DR   RefSeq; NP_463043.1; NC_003197.2.
DR   RefSeq; WP_000617942.1; NC_003197.2.
DR   PDB; 1OJL; X-ray; 3.00 A; A/B/C/D/E/F=141-441.
DR   PDBsum; 1OJL; -.
DR   AlphaFoldDB; P25852; -.
DR   SMR; P25852; -.
DR   STRING; 99287.STM4174; -.
DR   PaxDb; P25852; -.
DR   EnsemblBacteria; AAL23002; AAL23002; STM4174.
DR   GeneID; 1255700; -.
DR   KEGG; stm:STM4174; -.
DR   PATRIC; fig|99287.12.peg.4388; -.
DR   HOGENOM; CLU_000445_0_6_6; -.
DR   OMA; MPISMQV; -.
DR   PhylomeDB; P25852; -.
DR   BioCyc; SENT99287:STM4174-MON; -.
DR   EvolutionaryTrace; P25852; -.
DR   Proteomes; UP000001014; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0043565; F:sequence-specific DNA binding; IEA:InterPro.
DR   GO; GO:0000160; P:phosphorelay signal transduction system; IEA:UniProtKB-KW.
DR   GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:InterPro.
DR   Gene3D; 3.40.50.300; -; 1.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR011006; CheY-like_superfamily.
DR   InterPro; IPR009057; Homeobox-like_sf.
DR   InterPro; IPR002197; HTH_Fis.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR   InterPro; IPR002078; Sigma_54_int.
DR   InterPro; IPR025662; Sigma_54_int_dom_ATP-bd_1.
DR   InterPro; IPR025943; Sigma_54_int_dom_ATP-bd_2.
DR   InterPro; IPR025944; Sigma_54_int_dom_CS.
DR   Pfam; PF02954; HTH_8; 1.
DR   Pfam; PF00072; Response_reg; 1.
DR   Pfam; PF00158; Sigma54_activat; 1.
DR   PRINTS; PR01590; HTHFIS.
DR   SMART; SM00382; AAA; 1.
DR   SMART; SM00448; REC; 1.
DR   SUPFAM; SSF46689; SSF46689; 1.
DR   SUPFAM; SSF52172; SSF52172; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   PROSITE; PS50110; RESPONSE_REGULATORY; 1.
DR   PROSITE; PS00675; SIGMA54_INTERACT_1; 1.
DR   PROSITE; PS00676; SIGMA54_INTERACT_2; 1.
DR   PROSITE; PS00688; SIGMA54_INTERACT_3; 1.
DR   PROSITE; PS50045; SIGMA54_INTERACT_4; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Activator; ATP-binding; Cytoplasm; DNA-binding;
KW   Nucleotide-binding; Phosphoprotein; Reference proteome; Transcription;
KW   Transcription regulation; Two-component regulatory system.
FT   CHAIN           1..441
FT                   /note="Transcriptional regulatory protein ZraR"
FT                   /id="PRO_0000081283"
FT   DOMAIN          7..121
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00169"
FT   DOMAIN          141..370
FT                   /note="Sigma-54 factor interaction"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00193"
FT   DNA_BIND        421..440
FT                   /note="H-T-H motif"
FT                   /evidence="ECO:0000250"
FT   BINDING         169..176
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00193"
FT   BINDING         232..241
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00193"
FT   MOD_RES         56
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00169"
FT   CONFLICT        159
FT                   /note="A -> R (in Ref. 1; AAA27149)"
FT                   /evidence="ECO:0000305"
FT   HELIX           146..158
FT                   /evidence="ECO:0007829|PDB:1OJL"
FT   STRAND          165..169
FT                   /evidence="ECO:0007829|PDB:1OJL"
FT   HELIX           175..185
FT                   /evidence="ECO:0007829|PDB:1OJL"
FT   STRAND          189..191
FT                   /evidence="ECO:0007829|PDB:1OJL"
FT   STRAND          195..197
FT                   /evidence="ECO:0007829|PDB:1OJL"
FT   HELIX           203..210
FT                   /evidence="ECO:0007829|PDB:1OJL"
FT   HELIX           228..232
FT                   /evidence="ECO:0007829|PDB:1OJL"
FT   STRAND          235..241
FT                   /evidence="ECO:0007829|PDB:1OJL"
FT   HELIX           247..258
FT                   /evidence="ECO:0007829|PDB:1OJL"
FT   STRAND          259..261
FT                   /evidence="ECO:0007829|PDB:1OJL"
FT   STRAND          276..283
FT                   /evidence="ECO:0007829|PDB:1OJL"
FT   HELIX           285..291
FT                   /evidence="ECO:0007829|PDB:1OJL"
FT   HELIX           296..302
FT                   /evidence="ECO:0007829|PDB:1OJL"
FT   STRAND          303..308
FT                   /evidence="ECO:0007829|PDB:1OJL"
FT   HELIX           313..318
FT                   /evidence="ECO:0007829|PDB:1OJL"
FT   HELIX           319..333
FT                   /evidence="ECO:0007829|PDB:1OJL"
FT   HELIX           343..351
FT                   /evidence="ECO:0007829|PDB:1OJL"
FT   HELIX           357..371
FT                   /evidence="ECO:0007829|PDB:1OJL"
FT   STRAND          374..377
FT                   /evidence="ECO:0007829|PDB:1OJL"
FT   HELIX           379..381
FT                   /evidence="ECO:0007829|PDB:1OJL"
FT   HELIX           384..386
FT                   /evidence="ECO:0007829|PDB:1OJL"
FT   HELIX           402..415
FT                   /evidence="ECO:0007829|PDB:1OJL"
FT   TURN            416..419
FT                   /evidence="ECO:0007829|PDB:1OJL"
FT   HELIX           421..428
FT                   /evidence="ECO:0007829|PDB:1OJL"
FT   HELIX           432..438
FT                   /evidence="ECO:0007829|PDB:1OJL"
SQ   SEQUENCE   441 AA;  48590 MW;  5753C4E54F8C52F5 CRC64;
     MIRGKIDILV VDDDVSHCTI LQALLRGWGY NVALAYSGHD ALAQVREKVF DLVLCDVRMA
     EMDGIATLKE IKALNPAIPI LIMTAFSSVE TAVEALKAGA LDYLIKPLDF DRLQETLEKA
     LAHTRETGAE LPSASAAQFG MIGSSPAMQH LLNEIAMVAP SDATVLIHGD SGTGKELVAR
     ALHACSARSD RPLVTLNCAA LNESLLESEL FGHEKGAFTG ADKRREGRFV EADGGTLFLD
     EIGDISPLMQ VRLLRAIQER EVQRVGSNQT ISVDVRLIAA THRDLAEEVS AGRFRQDLYY
     RLNVVAIEMP SLRQRREDIP LLADHFLRRF AERNRKVVKG FTPQAMDLLI HYDWPGNIRE
     LENAIERAVV LLTGEYISER ELPLAIAATP IKTEYSGEIQ PLVDVEKEVI LAALEKTGGN
     KTEAARQLGI TRKTLLAKLS R
 
 
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