(data stored in SCRATCH zone)

SWISSPROT: Q13HL8_PARXL

ID   Q13HL8_PARXL            Unreviewed;      1344 AA.
AC   Q13HL8;
DT   22-AUG-2006, integrated into UniProtKB/TrEMBL.
DT   22-AUG-2006, sequence version 1.
DT   08-MAY-2019, entry version 108.
DE   SubName: Full=Multi sensor hybrid histidine kinase {ECO:0000313|EMBL:ABE36421.1};
DE            EC=2.7.3.- {ECO:0000313|EMBL:ABE36421.1};
GN   ORFNames=Bxe_C0521 {ECO:0000313|EMBL:ABE36421.1};
OS   Paraburkholderia xenovorans (strain LB400).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Paraburkholderia.
OX   NCBI_TaxID=266265 {ECO:0000313|EMBL:ABE36421.1, ECO:0000313|Proteomes:UP000001817};
RN   [1] {ECO:0000313|EMBL:ABE36421.1, ECO:0000313|Proteomes:UP000001817}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LB400 {ECO:0000313|EMBL:ABE36421.1,
RC   ECO:0000313|Proteomes:UP000001817};
RX   PubMed=17030797; DOI=10.1073/pnas.0606924103;
RA   Chain P.S., Denef V.J., Konstantinidis K.T., Vergez L.M., Agullo L.,
RA   Reyes V.L., Hauser L., Cordova M., Gomez L., Gonzalez M., Land M.,
RA   Lao V., Larimer F., LiPuma J.J., Mahenthiralingam E., Malfatti S.A.,
RA   Marx C.J., Parnell J.J., Ramette A., Richardson P., Seeger M.,
RA   Smith D., Spilker T., Sul W.J., Tsoi T.V., Ulrich L.E., Zhulin I.B.,
RA   Tiedje J.M.;
RT   "Burkholderia xenovorans LB400 harbors a multi-replicon, 9.73-Mbp
RT   genome shaped for versatility.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:15280-15287(2006).
CC   -!- FUNCTION: Involved in chemotaxis. Part of a chemotaxis signal
CC       transduction system that modulates chemotaxis in response to
CC       various stimuli. Catalyzes the demethylation of specific
CC       methylglutamate residues introduced into the chemoreceptors
CC       (methyl-accepting chemotaxis proteins or MCP) by CheR. Also
CC       mediates the irreversible deamidation of specific glutamine
CC       residues to glutamic acid. {ECO:0000256|SAAS:SAAS01100814}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + L-glutaminyl-[protein] = L-glutamyl-[protein] +
CC         NH4(+); Xref=Rhea:RHEA:16441, Rhea:RHEA-COMP:10207, Rhea:RHEA-
CC         COMP:10208, ChEBI:CHEBI:15377, ChEBI:CHEBI:28938,
CC         ChEBI:CHEBI:29973, ChEBI:CHEBI:30011; EC=3.5.1.44;
CC         Evidence={ECO:0000256|SAAS:SAAS01116312};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[protein]-L-glutamate 5-O-methyl ester + H2O = H(+) + L-
CC         glutamyl-[protein] + methanol; Xref=Rhea:RHEA:23236, Rhea:RHEA-
CC         COMP:10208, Rhea:RHEA-COMP:10311, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:17790, ChEBI:CHEBI:29973,
CC         ChEBI:CHEBI:82795; EC=3.1.1.61;
CC         Evidence={ECO:0000256|SAAS:SAAS01130167};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|SAAS:SAAS00132521}.
CC   -!- SIMILARITY: Belongs to the CheB family.
CC       {ECO:0000256|SAAS:SAAS01100824}.
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DR   EMBL; CP000272; ABE36421.1; -; Genomic_DNA.
DR   RefSeq; WP_011493677.1; NZ_CP008761.1.
DR   STRING; 266265.Bxe_C0521; -.
DR   EnsemblBacteria; ABE36421; ABE36421; Bxe_C0521.
DR   GeneID; 4010035; -.
DR   KEGG; bxb:DR64_7925; -.
DR   KEGG; bxe:Bxe_C0521; -.
DR   PATRIC; fig|266265.5.peg.8281; -.
DR   eggNOG; ENOG4105BZU; Bacteria.
DR   eggNOG; COG1352; LUCA.
DR   eggNOG; COG2201; LUCA.
DR   HOGENOM; HOG000062543; -.
DR   KO; K13924; -.
DR   OMA; SHELKHP; -.
DR   OrthoDB; 1755994at2; -.
DR   BioCyc; BXEN266265:BXE_RS39130-MONOMER; -.
DR   Proteomes; UP000001817; Chromosome 3.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0000156; F:phosphorelay response regulator activity; IEA:InterPro.
DR   GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR   GO; GO:0008984; F:protein-glutamate methylesterase activity; IEA:UniProtKB-EC.
DR   GO; GO:0050568; F:protein-glutamine glutaminase activity; IEA:UniProtKB-EC.
DR   GO; GO:0008757; F:S-adenosylmethionine-dependent methyltransferase activity; IEA:InterPro.
DR   GO; GO:0006935; P:chemotaxis; IEA:UniProtKB-UniRule.
DR   CDD; cd00075; HATPase_c; 1.
DR   CDD; cd00082; HisKA; 1.
DR   CDD; cd00130; PAS; 1.
DR   CDD; cd00156; REC; 1.
DR   Gene3D; 3.30.565.10; -; 1.
DR   Gene3D; 3.40.50.180; -; 1.
DR   InterPro; IPR035909; CheB_C.
DR   InterPro; IPR022642; CheR_C.
DR   InterPro; IPR000780; CheR_MeTrfase.
DR   InterPro; IPR022641; CheR_N.
DR   InterPro; IPR011006; CheY-like_superfamily.
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; IPR000700; PAS-assoc_C.
DR   InterPro; IPR035965; PAS-like_dom_sf.
DR   InterPro; IPR013656; PAS_4.
DR   InterPro; IPR029063; SAM-dependent_MTases.
DR   InterPro; IPR000673; Sig_transdc_resp-reg_Me-estase.
DR   InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR   Pfam; PF01339; CheB_methylest; 1.
DR   Pfam; PF01739; CheR; 1.
DR   Pfam; PF03705; CheR_N; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00512; HisKA; 1.
DR   Pfam; PF08448; PAS_4; 1.
DR   Pfam; PF00072; Response_reg; 1.
DR   PRINTS; PR00996; CHERMTFRASE.
DR   SMART; SM00387; HATPase_c; 1.
DR   SMART; SM00388; HisKA; 1.
DR   SMART; SM00138; MeTrc; 1.
DR   SMART; SM00091; PAS; 3.
DR   SMART; SM00448; REC; 1.
DR   SUPFAM; SSF47384; SSF47384; 1.
DR   SUPFAM; SSF52172; SSF52172; 1.
DR   SUPFAM; SSF52738; SSF52738; 1.
DR   SUPFAM; SSF53335; SSF53335; 1.
DR   SUPFAM; SSF55785; SSF55785; 2.
DR   SUPFAM; SSF55874; SSF55874; 1.
DR   TIGRFAMs; TIGR00229; sensory_box; 1.
DR   PROSITE; PS50122; CHEB; 1.
DR   PROSITE; PS50123; CHER; 1.
DR   PROSITE; PS50109; HIS_KIN; 1.
DR   PROSITE; PS50113; PAC; 1.
DR   PROSITE; PS50112; PAS; 1.
DR   PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q13HL8.
DR   SWISS-2DPAGE; Q13HL8.
KW   Chemotaxis {ECO:0000256|PROSITE-ProRule:PRU00050,
KW   ECO:0000256|SAAS:SAAS00706681}; Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001817};
KW   Cytoplasm {ECO:0000256|SAAS:SAAS00132526};
KW   Hydrolase {ECO:0000256|PROSITE-ProRule:PRU00050,
KW   ECO:0000256|SAAS:SAAS00706700}; Kinase {ECO:0000313|EMBL:ABE36421.1};
KW   Phosphoprotein {ECO:0000256|PROSITE-ProRule:PRU00169};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001817};
KW   Transferase {ECO:0000313|EMBL:ABE36421.1}.
FT   DOMAIN       13    203       CheB-type methylesterase.
FT                                {ECO:0000259|PROSITE:PS50122}.
FT   DOMAIN      230    479       CheR-type methyltransferase.
FT                                {ECO:0000259|PROSITE:PS50123}.
FT   DOMAIN      842    912       PAS. {ECO:0000259|PROSITE:PS50112}.
FT   DOMAIN      915    967       PAC. {ECO:0000259|PROSITE:PS50113}.
FT   DOMAIN      985   1202       Histidine kinase. {ECO:0000259|PROSITE:
FT                                PS50109}.
FT   DOMAIN     1223   1339       Response regulatory.
FT                                {ECO:0000259|PROSITE:PS50110}.
FT   COILED      661    716       {ECO:0000256|SAM:Coils}.
FT   ACT_SITE     25     25       {ECO:0000256|PROSITE-ProRule:PRU00050}.
FT   ACT_SITE     53     53       {ECO:0000256|PROSITE-ProRule:PRU00050}.
FT   ACT_SITE    145    145       {ECO:0000256|PROSITE-ProRule:PRU00050}.
FT   MOD_RES    1272   1272       4-aspartylphosphate.
FT                                {ECO:0000256|PROSITE-ProRule:PRU00169}.
SQ   SEQUENCE   1344 AA;  146057 MW;  531C452160460AA8 CRC64;
     MNDASNISPT PGAATGPRIV AIGASAGALH ALSLFFRAAC TIPHDIAFAV VVHLAPGAES
     HLPELLAKDT SFAVSAIEDG ATLRPGHVYV IPPKVSVVIE QGAFRLRPAV ERPTIPMPID
     AFFTSLATDQ HDRAIGIVLT GANADGSAGL RAIKAAGGMV MAQAPETAEH DSMPTHAIAT
     GLVDYVLPVE KMPAVLFDYI ARSTEEMSSV SGKLEVQTDL EPVLRALAAA GSDFRGYKRG
     TLGRRIARRM AVNQVDSLDA YCEILRTSVE EAQALSLDMM IGVTEFFRDP EAWKALAERV
     VDSLLGEQKG DQPLRIWVPG CATGEEAYSM AMLLTEEIEK RKITRSFMIL ASDVNRIALA
     RARQGIYPPG VALPVGEERL ERFFRAHGDG YQIDQALRET ILFTPQNLIA DPPFSRVDLI
     SCRNLLIYLE PAAQQRVFEV FHFALNPKRY LFLGRSESTD PDSSQFQEVS RTWRIYQRSP
     AATAVVSGYR FSATGGRREE FPSASRGGAR SKGYAELVNG TLLAEHHAAS VLINSAHQVL
     YVSGSTDEYL RQPAGEPTGN ILDMAREGLR LKLRIVLRRA TQDQTVSPVS EVVSDGGAPG
     VKITVTQPFD TAHTGKALLV VFARVAVADR PASLAPTGVD SDLWHLESEL RTTQVELGST
     IEELEESNSE LRVSNEEILS MNEELRSANE ELETSKEELQ ALNEQLNVVN SQLGQKVHEL
     EMLSEDVTNL LASTEIATLL LDGHAVIKRF TPRAARIFGL ALADIDRPIT NVLGNPLGDA
     LLEDVQRVLS AQTGQAEKEI ETVTGEWYVR RITPYIAVKG ASPAGVVVTW NDITHVKASD
     ERSRRLAAVV QDSNDAMTVF DLNGRLMAWN RAATAMYGYT EAEALGMTVS DMLPPGARQD
     HLDFIRYAAH NEALHSYETQ RVTKGGRVVD IWITLSILSD DQGHAVAIAT TERELTDRSL
     SNAQLRERAE RLAQADRRKN EFLAMLGHEL RNPLAALCSS GDLLASETID PRQKSWAVGV
     IQRQGRSMTQ LVNEMLDLTR ITSGSIELRR QAVTLKAVIQ SAVEVCQPII DERHHTLSVS
     LPDEPVLMYV DPTRLSQVVE NIVINAARYT EPGGHISLTA TRTGRRLSLR VKDNGRGIPA
     SMLSTLFDMF VQGPVPYGQL HNGLGVGLSV VRRLVELHGG SVRAISDGRT GSEFIVDLPL
     GMIPPGVEQA GTPQEPVNAG PRKILIIDDN ADASEALAML LAAEGHVVET RLDGPGGLEA
     ASTFRPDVVL LDIGLPGMDG YEVAKQLRDS VATYDTMLIA VTGYGQPGDQ LRSAEAGLDY
     HLVKPVDINA LTRLLAVQVK PRGR
//

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