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PLEC_CAUVC
ID   PLEC_CAUVC              Reviewed;         842 AA.
AC   P37894;
DT   01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT   27-APR-2001, sequence version 2.
DT   03-AUG-2022, entry version 158.
DE   RecName: Full=Non-motile and phage-resistance protein;
DE            EC=2.7.13.3;
GN   Name=pleC; OrderedLocusNames=CC_2482;
OS   Caulobacter vibrioides (strain ATCC 19089 / CB15) (Caulobacter crescentus).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Caulobacterales;
OC   Caulobacteraceae; Caulobacter.
OX   NCBI_TaxID=190650;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 19089 / CB15;
RX   PubMed=8421698; DOI=10.1073/pnas.90.2.630;
RA   Wang S.P., Sharma P.L., Schoenlein P.V., Ely B.;
RT   "A histidine protein kinase is involved in polar organelle development in
RT   Caulobacter crescentus.";
RL   Proc. Natl. Acad. Sci. U.S.A. 90:630-634(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 19089 / CB15;
RX   PubMed=11259647; DOI=10.1073/pnas.061029298;
RA   Nierman W.C., Feldblyum T.V., Laub M.T., Paulsen I.T., Nelson K.E.,
RA   Eisen J.A., Heidelberg J.F., Alley M.R.K., Ohta N., Maddock J.R.,
RA   Potocka I., Nelson W.C., Newton A., Stephens C., Phadke N.D., Ely B.,
RA   DeBoy R.T., Dodson R.J., Durkin A.S., Gwinn M.L., Haft D.H., Kolonay J.F.,
RA   Smit J., Craven M.B., Khouri H.M., Shetty J., Berry K.J., Utterback T.R.,
RA   Tran K., Wolf A.M., Vamathevan J.J., Ermolaeva M.D., White O.,
RA   Salzberg S.L., Venter J.C., Shapiro L., Fraser C.M.;
RT   "Complete genome sequence of Caulobacter crescentus.";
RL   Proc. Natl. Acad. Sci. U.S.A. 98:4136-4141(2001).
RN   [3]
RP   PHOSPHORYLATION OF PLED.
RX   PubMed=15075296; DOI=10.1101/gad.289504;
RA   Paul R., Weiser S., Amiot N.C., Chan C., Schirmer T., Giese B., Jenal U.;
RT   "Cell cycle-dependent dynamic localization of a bacterial response
RT   regulator with a novel di-guanylate cyclase output domain.";
RL   Genes Dev. 18:715-727(2004).
CC   -!- FUNCTION: Member of the two-component regulatory system involved in the
CC       regulation of polar organelle development. PleC functions as a
CC       membrane-associated protein kinase that transfers phosphate to the
CC       response regulator PleD, leading to its activation.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + protein L-histidine = ADP + protein N-phospho-L-
CC         histidine.; EC=2.7.13.3;
CC   -!- INTERACTION:
CC       P37894; Q9A5I5: pleD; NbExp=4; IntAct=EBI-1784742, EBI-1784732;
CC       P37894; Q45976: divK; Xeno; NbExp=8; IntAct=EBI-1784742, EBI-1784754;
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC       protein {ECO:0000305}.
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DR   EMBL; M91449; AAA23052.1; -; Genomic_DNA.
DR   EMBL; AE005673; AAK24453.1; -; Genomic_DNA.
DR   PIR; A87557; A87557.
DR   PIR; S27533; S27533.
DR   RefSeq; NP_421285.1; NC_002696.2.
DR   RefSeq; WP_010920340.1; NC_002696.2.
DR   AlphaFoldDB; P37894; -.
DR   SMR; P37894; -.
DR   DIP; DIP-44286N; -.
DR   IntAct; P37894; 3.
DR   MINT; P37894; -.
DR   STRING; 190650.CC_2482; -.
DR   PRIDE; P37894; -.
DR   EnsemblBacteria; AAK24453; AAK24453; CC_2482.
DR   KEGG; ccr:CC_2482; -.
DR   PATRIC; fig|190650.5.peg.2500; -.
DR   eggNOG; COG2202; Bacteria.
DR   eggNOG; COG2205; Bacteria.
DR   HOGENOM; CLU_000445_114_71_5; -.
DR   OMA; GFAFHWQ; -.
DR   BioCyc; CAULO:CC2482-MON; -.
DR   Proteomes; UP000001816; Chromosome.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0000155; F:phosphorelay sensor kinase activity; IDA:CACAO.
DR   GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR   GO; GO:0000160; P:phosphorelay signal transduction system; IDA:CACAO.
DR   GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:InterPro.
DR   CDD; cd00082; HisKA; 1.
DR   Gene3D; 3.30.565.10; -; 1.
DR   InterPro; IPR003594; HATPase_C.
DR   InterPro; IPR036890; HATPase_C_sf.
DR   InterPro; IPR005467; His_kinase_dom.
DR   InterPro; IPR003661; HisK_dim/P.
DR   InterPro; IPR036097; HisK_dim/P_sf.
DR   InterPro; IPR000014; PAS.
DR   InterPro; IPR035965; PAS-like_dom_sf.
DR   InterPro; IPR013767; PAS_fold.
DR   InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00512; HisKA; 1.
DR   Pfam; PF00989; PAS; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00387; HATPase_c; 1.
DR   SMART; SM00388; HisKA; 1.
DR   SMART; SM00091; PAS; 2.
DR   SUPFAM; SSF47384; SSF47384; 1.
DR   SUPFAM; SSF55785; SSF55785; 2.
DR   SUPFAM; SSF55874; SSF55874; 1.
DR   PROSITE; PS50109; HIS_KIN; 1.
DR   PROSITE; PS50112; PAS; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Cell cycle; Cell membrane; Differentiation; Kinase; Membrane;
KW   Nucleotide-binding; Phosphoprotein; Reference proteome; Transferase;
KW   Transmembrane; Transmembrane helix; Two-component regulatory system.
FT   CHAIN           1..842
FT                   /note="Non-motile and phage-resistance protein"
FT                   /id="PRO_0000074852"
FT   TRANSMEM        29..50
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        283..303
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        343..363
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          318..389
FT                   /note="PAS"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00140"
FT   DOMAIN          607..830
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
FT   MOD_RES         610
FT                   /note="Phosphohistidine; by autocatalysis"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
FT   CONFLICT        744
FT                   /note="A -> V (in Ref. 1; AAA23052)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   842 AA;  89560 MW;  DCFF4F092DE2CBF8 CRC64;
     MGRHGGPAAA GPTAPSAVRA KAVNAPSQVF VRIAILAALL LLAVYTAFGV HRLQREAMAQ
     PGGAPLAAKA DLIAGRVDAN LAAQRAGLSA AADLLKRDPG ATMDAAETTL RAAGGEAAAV
     AVVSEAGVVA VAGRDDGADW KAAALAAGAS GRTNWVGSVG ETGRLYVATT TSLDRARAFV
     IASGDASRLV ADPEKGESGA LALPDGKLIA ARGRGVQGAG ALREAFALSI EDLGDGPAAV
     RGQAADGALL DVAVRPVAQG ALLAVAAAPT RSVANLDRQV MEGAFSLLVP LGVGIALALL
     LMIQSRKAEV AHREFIDSER RFRLAVEAAR CGIWEWDLNG DQVYLSDVTG AMFGWGGGGV
     VSGQDLLERI SIDHRERVRQ ALANAAMYGA FDVSFRVPAS EQGARSLWID ARGQGFGKPG
     SEGHARIIGV ALDVTEERIA QARAQAAENR LRDAIESVSE AFVLWDRQGR LLMCNRNYRS
     VFSLEPKILK PGAARAEVNR FAALAIKQDH PAPDGAKGVR EAEMMDGRWI QISERRTAEG
     GLVMTAADIT AIKTQEEARR RNEEQLQNAV AGLERSQEQL AELARKYETE KVKAESANKA
     KSEFLANMSH ELRTPLNAIN GFSEIMMNEM FGPLGDQRYK GYSQDIHSSG QHLLALINDI
     LDMSKIEAGK MNLKFESMHL EDVAEDAVRL VRNRAEAAGL KLDIDFPQLP EIEADYRAVK
     QVLLNLLSNA IKFTPRAGSV TVRAEVRRDP FGDLIKVSVT DTGIGIAKED LARLAKPFEQ
     VESQFSKTTQ GTGLGLALTK SLITMHDGVL EMHSTPGEGT TVSFTLPVRH SDQKITRDFV
     AA
 
 
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