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ALKS_PSEOL
ID   ALKS_PSEOL              Reviewed;         882 AA.
AC   P17051;
DT   01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT   30-MAY-2000, sequence version 3.
DT   03-AUG-2022, entry version 98.
DE   RecName: Full=HTH-type transcriptional regulator AlkS;
GN   Name=alkS;
OS   Pseudomonas oleovorans.
OG   Plasmid OCT.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas;
OC   Pseudomonas oleovorans/pseudoalcaligenes group.
OX   NCBI_TaxID=301;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC   STRAIN=ATCC 29347 / CIP 105816 / NRRL B-14683 / TF4-1L;
RX   PubMed=10347009; DOI=10.1128/aem.65.6.2324-2332.1999;
RA   Panke S., Meyer A., Huber C.M., Witholt B., Wubbolts M.G.;
RT   "An alkane-responsive expression system for the production of fine
RT   chemicals.";
RL   Appl. Environ. Microbiol. 65:2324-2332(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 659-882.
RC   STRAIN=ATCC 29347 / CIP 105816 / NRRL B-14683 / TF4-1L;
RX   PubMed=2319593; DOI=10.1016/0022-2836(90)90310-i;
RA   Eggink G., Engel H., Vriend G., Terpstra P., Witholt B.;
RT   "Rubredoxin reductase of Pseudomonas oleovorans. Structural relationship to
RT   other flavoprotein oxidoreductases based on one NAD and two FAD
RT   fingerprints.";
RL   J. Mol. Biol. 212:135-142(1990).
RN   [3]
RP   FUNCTION, AND INDUCTION.
RX   PubMed=10692156; DOI=10.1046/j.1365-2958.2000.01751.x;
RA   Canosa I., Sanchez-Romero J.M., Yuste L., Rojo F.;
RT   "A positive feedback mechanism controls expression of AlkS, the
RT   transcriptional regulator of the Pseudomonas oleovorans alkane degradation
RT   pathway.";
RL   Mol. Microbiol. 35:791-799(2000).
CC   -!- FUNCTION: This protein activates the expression of alkBFGHJKL operon in
CC       the presence of alkanes. {ECO:0000269|PubMed:10347009,
CC       ECO:0000269|PubMed:10692156}.
CC   -!- PATHWAY: Hydrocarbon metabolism; alkane degradation.
CC   -!- INDUCTION: Protein expression is autoregulated and sigma S-dependent in
CC       stationary phase. {ECO:0000269|PubMed:10692156}.
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DR   EMBL; AJ245436; CAB54064.1; -; Genomic_DNA.
DR   PIR; S09113; S09113.
DR   AlphaFoldDB; P17051; -.
DR   SMR; P17051; -.
DR   KEGG; ag:CAB54064; -.
DR   UniPathway; UPA00191; -.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0043448; P:alkane catabolic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:InterPro.
DR   CDD; cd06170; LuxR_C_like; 1.
DR   Gene3D; 1.10.10.10; -; 1.
DR   InterPro; IPR016032; Sig_transdc_resp-reg_C-effctor.
DR   InterPro; IPR000792; Tscrpt_reg_LuxR_C.
DR   InterPro; IPR036388; WH-like_DNA-bd_sf.
DR   Pfam; PF00196; GerE; 1.
DR   SMART; SM00421; HTH_LUXR; 1.
DR   SUPFAM; SSF46894; SSF46894; 1.
DR   PROSITE; PS50043; HTH_LUXR_2; 1.
PE   2: Evidence at transcript level;
KW   ATP-binding; DNA-binding; Nucleotide-binding; Plasmid; Transcription;
KW   Transcription regulation.
FT   CHAIN           1..882
FT                   /note="HTH-type transcriptional regulator AlkS"
FT                   /id="PRO_0000184139"
FT   DOMAIN          815..880
FT                   /note="HTH luxR-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00411"
FT   DNA_BIND        839..858
FT                   /note="H-T-H motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00411"
FT   BINDING         51..58
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   882 AA;  99770 MW;  414B9BCCDC607545 CRC64;
     MKIIINNDFP VAKVGADQIT TLVSAKVHSC IYRPRLSIAD GAAPRVCLYR APPGYGKTVA
     LAFEWLRHRT AGRPAVWLSL RASSYSEFDI CAEIIEQLET FEMVKFSRVR EGVSKPALLR
     DLASSLWQST SNNEIETLVC LDNINHDLDL PLLHALMEFM LNTPKNIRFA VAGNTIKGFS
     QLKLAGAMRE YTEKDLAFSA EEAVALAEAE SVLGVPEEQI ETLVQEVEGW PALVVFLLKR
     ELPAKHISAV VEVDNYFRDE IFEAIPERYR VFLANSSLLD FVTPDQYNYV FKCVNGVSCI
     KYLSTNYMLL RHVSGEPAQF TLHPVLRNFL REITWTENPA KRSYLLKRAA FWHWRRGEYQ
     YAIRISLRAN DCRWAVSMSE RIILDLSFRQ GEIDALRQWL LELPKQAWHQ KPIVLISYAW
     VLYFSQQGAR AEKLIKDLSS QSDKKNKWQE KEWLQLVLAI GKATKDEMLS SEELCNKWIS
     LFGDSNAVGK GAALTCLAFI FASEYRFAEL EKVLAQAQAV NKFAKQNFAF GWLYVARFQQ
     ALASGKMGWA RQIITQARTD SRAQMMESEF TSKMFDALEL ELHYELRCLD TSEEKLSKIL
     EFISNHGVTD VFFSVCRAVS AWRLGRSDLN GSIEILEWAK AHAVEKNLPR LEVMSQIEIY
     QRLVCQGITG INNLKTLEDH KIFSGQHSAP LKARLLLVQS LVLSRDRNFH SAAHRALLAI
     QQARKINAGQ LEVRGLLCLA GAQAGAGDLK KAQLNIVYAV EIAKQLQCFQ TVLDEVCLIE
     RIIPASCEAF TAVNLDQAIG AFSLPRIVEI GKSAENKADA LLTRKQIAVL RLVKEGCSNK
     QIATNMHVTE DAIKWHMRKI FATLNVVNRT QATIEAERQG II
 
 
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