GenomeNet

Database: UniProt
Entry: A0A1V2H4Y5_9PROT
LinkDB: A0A1V2H4Y5_9PROT
Original site: A0A1V2H4Y5_9PROT 
ID   A0A1V2H4Y5_9PROT        Unreviewed;      1320 AA.
AC   A0A1V2H4Y5;
DT   07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2017, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=BKE38_06830 {ECO:0000313|EMBL:ONG56119.1};
OS   Pseudoroseomonas deserti.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC   Acetobacteraceae; Pseudoroseomonas.
OX   NCBI_TaxID=1817963 {ECO:0000313|EMBL:ONG56119.1, ECO:0000313|Proteomes:UP000188879};
RN   [1] {ECO:0000313|EMBL:ONG56119.1, ECO:0000313|Proteomes:UP000188879}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=M3 {ECO:0000313|EMBL:ONG56119.1,
RC   ECO:0000313|Proteomes:UP000188879};
RA   Subhash Y., Lee S.;
RT   "Draft Genome sequence of Roseomonas sp. strain M3.";
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + protein L-histidine = ADP + protein N-phospho-L-
CC         histidine.; EC=2.7.13.3; Evidence={ECO:0000256|ARBA:ARBA00000085};
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00050}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:ONG56119.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; MLCO01000053; ONG56119.1; -; Genomic_DNA.
DR   OrthoDB; 5287260at2; -.
DR   Proteomes; UP000188879; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0000156; F:phosphorelay response regulator activity; IEA:InterPro.
DR   GO; GO:0004673; F:protein histidine kinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0008984; F:protein-glutamate methylesterase activity; IEA:InterPro.
DR   GO; GO:0008757; F:S-adenosylmethionine-dependent methyltransferase activity; IEA:InterPro.
DR   GO; GO:0006935; P:chemotaxis; IEA:InterPro.
DR   CDD; cd02440; AdoMet_MTases; 1.
DR   CDD; cd00130; PAS; 2.
DR   Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR   Gene3D; 3.40.50.180; Methylesterase CheB, C-terminal domain; 1.
DR   Gene3D; 3.30.450.20; PAS domain; 3.
DR   Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR   InterPro; IPR035909; CheB_C.
DR   InterPro; IPR022642; CheR_C.
DR   InterPro; IPR000780; CheR_MeTrfase.
DR   InterPro; IPR022641; CheR_N.
DR   InterPro; IPR036890; HATPase_C_sf.
DR   InterPro; IPR001610; PAC.
DR   InterPro; IPR000014; PAS.
DR   InterPro; IPR000700; PAS-assoc_C.
DR   InterPro; IPR035965; PAS-like_dom_sf.
DR   InterPro; IPR013656; PAS_4.
DR   InterPro; IPR013655; PAS_fold_3.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   InterPro; IPR011102; Sig_transdc_His_kinase_HWE.
DR   InterPro; IPR000673; Sig_transdc_resp-reg_Me-estase.
DR   NCBIfam; TIGR00229; sensory_box; 1.
DR   PANTHER; PTHR24422; CHEMOTAXIS PROTEIN METHYLTRANSFERASE; 1.
DR   PANTHER; PTHR24422:SF25; CHEMOTAXIS PROTEIN METHYLTRANSFERASE; 1.
DR   Pfam; PF01339; CheB_methylest; 1.
DR   Pfam; PF01739; CheR; 1.
DR   Pfam; PF03705; CheR_N; 1.
DR   Pfam; PF07536; HWE_HK; 1.
DR   Pfam; PF13596; PAS_10; 1.
DR   Pfam; PF08447; PAS_3; 1.
DR   Pfam; PF08448; PAS_4; 1.
DR   PRINTS; PR00996; CHERMTFRASE.
DR   SMART; SM00911; HWE_HK; 1.
DR   SMART; SM00138; MeTrc; 1.
DR   SMART; SM00086; PAC; 2.
DR   SMART; SM00091; PAS; 4.
DR   SUPFAM; SSF47757; Chemotaxis receptor methyltransferase CheR, N-terminal domain; 1.
DR   SUPFAM; SSF52738; Methylesterase CheB, C-terminal domain; 1.
DR   SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 3.
DR   SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR   PROSITE; PS50122; CHEB; 1.
DR   PROSITE; PS50123; CHER; 1.
DR   PROSITE; PS50113; PAC; 2.
DR   PROSITE; PS50112; PAS; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW   FMN {ECO:0000256|ARBA:ARBA00022643};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000188879};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          6..158
FT                   /note="CheB-type methylesterase"
FT                   /evidence="ECO:0000259|PROSITE:PS50122"
FT   DOMAIN          212..477
FT                   /note="CheR-type methyltransferase"
FT                   /evidence="ECO:0000259|PROSITE:PS50123"
FT   DOMAIN          914..966
FT                   /note="PAC"
FT                   /evidence="ECO:0000259|PROSITE:PS50113"
FT   DOMAIN          967..1037
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          1039..1092
FT                   /note="PAC"
FT                   /evidence="ECO:0000259|PROSITE:PS50113"
FT   REGION          141..170
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          482..511
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1299..1320
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          642..711
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        1304..1320
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1320 AA;  146802 MW;  EB5A8378BDFC5903 CRC64;
     MAPMMMEEAV PIVGIGVGTA SLRSLETVFA GLKSELGAAF LVAISHQGGL EVASVVRALE
     RQSPMPVQIG RNDLRVERDH VYVCGPDDMM TLQSGHLRIR PASEPVGHRG TIDTMLVSIA
     EQAHDRAVAV LLRGLGSAGT AGVTATKKSG GLSIGEADPG EDPQSDGAEG PLGVVDLRLP
     AERIATHIAI YLTNPANAGL EDGEPVAGEA MEAQVTRITT ILRNVTSHDF HSYKRGTFLR
     RVHRRMQVLQ IDSINGYVAR LRGDREEVQA LFQDLLIGVT QFFRDAQEFE VLEREIPRLF
     QGKTPDDQFR VWVLGCATGE EAYSIAILLR EHMATLAQPP QVQIFATDLD ARALGLARAG
     RYAASIADHI RPDRLARWFV REGDTYAVVK ELREMCIFSP HNLIKDAPFS RIDILSCRNL
     LIYLNADIQA RVIPIFHFSL RAGGVLFLGS SESVTRHQKL FTPVDRRNRV FRRLDTATRT
     VPDFPLSPRI RAPEPADSRN PDGAAGSRLS GSVSRQAEAI AERYAPAYVV VDRQYDILHF
     SGRTGRFLEP AAGAATLNLF SLVHRDLRIE LRAALHRAVS EAARVELPRL VLRHEEKPAG
     VNVIVQPVGE GDVTALVILF QDIGLLPEGP LRGDRLDHDE HVQRLENELR VTRDRLQATI
     EELETTNEEL KSSNEEYQSI NEELQSANEE METSKEELQS VNEELQTVNG ELAHRVAELG
     RSNSDLKNLL EATQIATVFL DNDLRVRSFT PTATEIFHLL ETDVGRPLGH VVSRVAYAEL
     QEDVRRVLKT LAPIERMVVD PAHDRHYAAK VLPYRSVDNY ISGAVVTFTD LTAVHKAETA
     LRESEQRLQA LLAASSEVIF RMSADWTEML DMWGGGFLAE LQDSRQWLAE LIPAEEHPRL
     ATELQAAVAE RRAFELEHSV FRVDGRPGWA VWRAVPITGP DGDIIEWFGA ASDITARREA
     EEAMRSSEQR LHSLVEGLPQ LVWRAREPGR WSWASRQWTD FTGQSDPDSL SWGWLEAVHP
     DDRHLARDAW ARAPEQGGFV SEFRLRHGRE GAYRWFQIRA TPVRDDQGAI LEWIGSCTDI
     DGLRGLQERQ TVLVAELQHR TRNLMAVVRK MAQKTARSSS DLDDFRERFR GRLDSLARVQ
     GLLSRLNEHD RVTFDELVQT ELAAHGAEPG ENHRVTVGGP LGVRLRSTTV QTLAMALHEL
     ATNAVKYGAL SQATAQLAIR WRIEMEAGAG AAMQPWLHVD WHESGVQMPA EPSAVQGSGQ
     GRELIERALP YQLDARTTYV VGEDGIRCTI AMPVSASNMV HENDDGLDGL EQPPNPDRRG
//
DBGET integrated database retrieval system