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HFQ_PSEAE
ID   HFQ_PSEAE               Reviewed;          82 AA.
AC   Q9HUM0;
DT   29-AUG-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   03-AUG-2022, entry version 119.
DE   RecName: Full=RNA-binding protein Hfq {ECO:0000255|HAMAP-Rule:MF_00436};
GN   Name=hfq {ECO:0000255|HAMAP-Rule:MF_00436}; OrderedLocusNames=PA4944;
OS   Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS   14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=208964;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC   PRS 101 / PAO1;
RX   PubMed=10984043; DOI=10.1038/35023079;
RA   Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA   Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA   Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA   Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA   Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA   Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT   "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT   pathogen.";
RL   Nature 406:959-964(2000).
CC   -!- FUNCTION: RNA chaperone that binds small regulatory RNA (sRNAs) and
CC       mRNAs to facilitate mRNA translational regulation in response to
CC       envelope stress, environmental stress and changes in metabolite
CC       concentrations. Also binds with high specificity to tRNAs.
CC       {ECO:0000255|HAMAP-Rule:MF_00436}.
CC   -!- SUBUNIT: Homohexamer. {ECO:0000255|HAMAP-Rule:MF_00436}.
CC   -!- SIMILARITY: Belongs to the Hfq family. {ECO:0000255|HAMAP-
CC       Rule:MF_00436}.
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DR   EMBL; AE004091; AAG08329.1; -; Genomic_DNA.
DR   PIR; D83028; D83028.
DR   RefSeq; NP_253631.1; NC_002516.2.
DR   RefSeq; WP_003095657.1; NZ_QZGE01000002.1.
DR   PDB; 1U1S; X-ray; 1.60 A; A/B/C/D/E/F=1-82.
DR   PDB; 1U1T; X-ray; 1.90 A; A/B/C/D/E/F=1-82.
DR   PDB; 3INZ; X-ray; 1.70 A; A/B/C/D/E/F=1-82.
DR   PDB; 3M4G; X-ray; 2.05 A; A/B/C/D/E/F/G/H/I/J/K/L=1-82.
DR   PDB; 3QUI; X-ray; 1.93 A; A/B/C/D/E/F=1-82.
DR   PDB; 4J5Y; X-ray; 2.10 A; A/B/C/D/E/F=1-82.
DR   PDB; 4J6W; X-ray; 1.80 A; A/B/C/D/E/F=1-82.
DR   PDB; 4J6X; X-ray; 2.22 A; A/B/C/D/E/F=1-82.
DR   PDB; 4J6Y; X-ray; 2.14 A; A/B/C/D/E/F=1-82.
DR   PDB; 4MMK; X-ray; 2.16 A; A/B/C/D/E/F/G/H/I/J/K/L=1-82.
DR   PDB; 4MML; X-ray; 1.80 A; A=1-82.
DR   PDB; 6O1K; EM; 3.13 A; C/D/E/F/G/H/I/J/K/L/M/N=5-71.
DR   PDB; 6O1L; EM; 3.37 A; C/D/E/F/G/H/I/J/K/L/M/N=5-71.
DR   PDB; 6O1M; EM; 3.15 A; C/D/E/F/G/H/I/J/K/L/M/N=5-71.
DR   PDB; 6XYJ; X-ray; 2.77 A; AAA/BBB/CCC/DDD/EEE/FFF=1-82.
DR   PDBsum; 1U1S; -.
DR   PDBsum; 1U1T; -.
DR   PDBsum; 3INZ; -.
DR   PDBsum; 3M4G; -.
DR   PDBsum; 3QUI; -.
DR   PDBsum; 4J5Y; -.
DR   PDBsum; 4J6W; -.
DR   PDBsum; 4J6X; -.
DR   PDBsum; 4J6Y; -.
DR   PDBsum; 4MMK; -.
DR   PDBsum; 4MML; -.
DR   PDBsum; 6O1K; -.
DR   PDBsum; 6O1L; -.
DR   PDBsum; 6O1M; -.
DR   PDBsum; 6XYJ; -.
DR   AlphaFoldDB; Q9HUM0; -.
DR   SMR; Q9HUM0; -.
DR   STRING; 287.DR97_2297; -.
DR   PaxDb; Q9HUM0; -.
DR   PRIDE; Q9HUM0; -.
DR   EnsemblBacteria; AAG08329; AAG08329; PA4944.
DR   GeneID; 878015; -.
DR   KEGG; pae:PA4944; -.
DR   PATRIC; fig|208964.12.peg.5177; -.
DR   PseudoCAP; PA4944; -.
DR   HOGENOM; CLU_113688_2_2_6; -.
DR   InParanoid; Q9HUM0; -.
DR   OMA; QQMVYKH; -.
DR   PhylomeDB; Q9HUM0; -.
DR   BioCyc; PAER208964:G1FZ6-5060-MON; -.
DR   EvolutionaryTrace; Q9HUM0; -.
DR   Proteomes; UP000002438; Chromosome.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR   GO; GO:0009372; P:quorum sensing; IMP:PseudoCAP.
DR   GO; GO:0043609; P:regulation of carbon utilization; IDA:PseudoCAP.
DR   GO; GO:0043487; P:regulation of RNA stability; IMP:PseudoCAP.
DR   GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:InterPro.
DR   GO; GO:0006417; P:regulation of translation; IDA:PseudoCAP.
DR   GO; GO:0045974; P:regulation of translation, ncRNA-mediated; IDA:PseudoCAP.
DR   CDD; cd01716; Hfq; 1.
DR   HAMAP; MF_00436; Hfq; 1.
DR   InterPro; IPR005001; Hfq.
DR   InterPro; IPR010920; LSM_dom_sf.
DR   PANTHER; PTHR34772; PTHR34772; 1.
DR   Pfam; PF17209; Hfq; 1.
DR   SUPFAM; SSF50182; SSF50182; 1.
DR   TIGRFAMs; TIGR02383; Hfq; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Reference proteome; RNA-binding; Stress response.
FT   CHAIN           1..82
FT                   /note="RNA-binding protein Hfq"
FT                   /id="PRO_0000095656"
FT   TURN            4..7
FT                   /evidence="ECO:0007829|PDB:3QUI"
FT   HELIX           8..17
FT                   /evidence="ECO:0007829|PDB:1U1S"
FT   STRAND          22..26
FT                   /evidence="ECO:0007829|PDB:1U1S"
FT   STRAND          31..39
FT                   /evidence="ECO:0007829|PDB:1U1S"
FT   STRAND          41..50
FT                   /evidence="ECO:0007829|PDB:1U1S"
FT   STRAND          52..55
FT                   /evidence="ECO:0007829|PDB:1U1S"
FT   HELIX           56..58
FT                   /evidence="ECO:0007829|PDB:1U1S"
FT   STRAND          59..66
FT                   /evidence="ECO:0007829|PDB:1U1S"
SQ   SEQUENCE   82 AA;  9104 MW;  1153661DC4C5AE2F CRC64;
     MSKGHSLQDP YLNTLRKERV PVSIYLVNGI KLQGQIESFD QFVILLKNTV SQMVYKHAIS
     TVVPSRPVRL PSGDQPAEPG NA
 
 
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