ID A0A1C2HBC2_9RHOB Unreviewed; 1130 AA.
AC A0A1C2HBC2;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=BFP70_16100 {ECO:0000313|EMBL:OCX60987.1};
OS Thioclava sp. SK-1.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Thioclava.
OX NCBI_TaxID=1889770 {ECO:0000313|EMBL:OCX60987.1, ECO:0000313|Proteomes:UP000094269};
RN [1] {ECO:0000313|EMBL:OCX60987.1, ECO:0000313|Proteomes:UP000094269}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SK-1 {ECO:0000313|EMBL:OCX60987.1,
RC ECO:0000313|Proteomes:UP000094269};
RA Wong S.-K., Hamasaki K., Yoshizawa S.;
RT "Draft genome of Thioclava sp. strain SK-1.";
RL Submitted (AUG-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: 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:OCX60987.1}.
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DR EMBL; MDHA01000069; OCX60987.1; -; Genomic_DNA.
DR RefSeq; WP_066012721.1; NZ_MDHA01000069.1.
DR AlphaFoldDB; A0A1C2HBC2; -.
DR STRING; 1889770.BFP70_16100; -.
DR OrthoDB; 9816309at2; -.
DR Proteomes; UP000094269; 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:InterPro.
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:UniProtKB-UniRule.
DR CDD; cd16434; CheB-CheR_fusion; 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; IPR035965; PAS-like_dom_sf.
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 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 PRINTS; PR00996; CHERMTFRASE.
DR SMART; SM00911; HWE_HK; 1.
DR SMART; SM00138; MeTrc; 1.
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); 1.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR PROSITE; PS50122; CHEB; 1.
DR PROSITE; PS50123; CHER; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Chemotaxis {ECO:0000256|PROSITE-ProRule:PRU00050};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Hydrolase {ECO:0000256|PROSITE-ProRule:PRU00050};
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:UP000094269};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 12..195
FT /note="CheB-type methylesterase"
FT /evidence="ECO:0000259|PROSITE:PS50122"
FT DOMAIN 210..448
FT /note="CheR-type methyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS50123"
FT COILED 628..694
FT /evidence="ECO:0000256|SAM:Coils"
FT ACT_SITE 18
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00050"
FT ACT_SITE 45
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00050"
FT ACT_SITE 137
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00050"
SQ SEQUENCE 1130 AA; 126139 MW; 77740CBA7838C809 CRC64;
MNTQTQHGRL GIVGVGASAG GLDALRAMLN TADPAGAISY VIVQHLDPDH SSLLAELLAR
QTRLKVVQAQ TGDIMCAGKV FIIPPNHGLR IANSRLELTD LKHIRGVRRT IDEFLESLAV
DQGSWAAGVI LSGTGTDGSR GLRSIKEHGG ICIAQHGESA KHDGMPLAAQ RTGSVDYIRL
PEDICPSLEQ YFAAMRRDPG DQSQIVAQSL SDICAVVDHC CGHDFSQYKR STLIRRVLRR
MQLSDLSDPL AYLRSLRSDV GQCQALYQDL LINMTRFFRD TAYFDALHDQ VLRPMVQGAQ
RDLRLWVAGC SSGEEAYSIA MLVAEEIRVQ QRKIDFQIFA TDIDDTMLNM ARAGQYSLSA
LPDIPETLRD RYAVLGNDVF TVSEAVRSRV RFSHHSVVRD APFAEVDLIS CRNLLIYFET
NLQNLAFPAF HHALRTGGTL FLGSSETLGQ YESFFAPIDV HARLFRKVDA QLDLPVLGQQ
EPRPIVPKLA AVPLPAQKAD PVLSRLLQAY APPSLRVNHY GEVIRATGKL SKYLAATPEP
RETVFATSVA LPGVREPISA AVRKVNDTGR RVILRDLIAR SEFGHQAFEL IAEPVGDDAI
LLVFRERDRF AALDDDDLEE FQASDDDVRG LEDDLRETRD RLNTTVEELE TANEELKSSN
EEMMSMNEEL QSTNEELATV NDELKSKVDE LSVANADLSN FFSSTSLPLI VLDRAMRIRN
FTNAIDGIYP FRQGDRGRPL SEVTSKLANP ADVTEAVELV MSTSQTQHRR VRSLTSGQTW
SLVVTPYFRD EDTCDGATLV FTELTEALRL EAALRSEGER LRLALDVANM GVWEFNPADD
GLQFDDTAAR LLWLKNNTVT VSDFFQHVTE KDRPEVMRQM LLKDGEDDEI DFRFSVDHMG
QARTLHFVGR RVSSARETRY LGVLFDVTAE DEAVRIREMM LREMNHRVKN MFSIISGMIR
IAGRSTREVP QLVEGIERRI NALARSHDMT QRAAKGRHMK VTLNEVLSMT LSPYVGHSKI
EMDGPEVSVE SHDLTALSLI FHEWATNASK YGVLGPLTGD LMINWQKNGE EITLEWNETY
EARIEPVKTT AGFGSTLVQL SAAQLHGSVS TDTSLTQRRM ILTYEPELAQ
//
