ID A0A0T5NRT1_9RHOB Unreviewed; 337 AA.
AC A0A0T5NRT1;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=XM53_14915 {ECO:0000313|EMBL:KRS11569.1};
OS Roseovarius atlanticus.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Roseovarius.
OX NCBI_TaxID=1641875 {ECO:0000313|EMBL:KRS11569.1, ECO:0000313|Proteomes:UP000051295};
RN [1] {ECO:0000313|EMBL:KRS11569.1, ECO:0000313|Proteomes:UP000051295}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=R12B {ECO:0000313|EMBL:KRS11569.1,
RC ECO:0000313|Proteomes:UP000051295};
RA Li G., Lai Q., Shao Z., Yan P.;
RT "The draft genome sequence of Roseovarius sp.R12b.";
RL Submitted (APR-2015) 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:KRS11569.1}.
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; LAXJ01000018; KRS11569.1; -; Genomic_DNA.
DR RefSeq; WP_057794709.1; NZ_LAXJ01000018.1.
DR AlphaFoldDB; A0A0T5NRT1; -.
DR STRING; 1641875.XM53_14915; -.
DR PATRIC; fig|1641875.4.peg.790; -.
DR OrthoDB; 9816309at2; -.
DR Proteomes; UP000051295; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004673; F:protein histidine kinase activity; IEA:InterPro.
DR CDD; cd00130; PAS; 1.
DR Gene3D; 2.10.70.100; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 3.30.450.20; PAS domain; 1.
DR InterPro; IPR036890; HATPase_C_sf.
DR InterPro; IPR000014; PAS.
DR InterPro; IPR000700; PAS-assoc_C.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR013655; PAS_fold_3.
DR InterPro; IPR011102; Sig_transdc_His_kinase_HWE.
DR PANTHER; PTHR41523:SF7; ETHYLENE RESPONSE SENSOR PROTEIN; 1.
DR PANTHER; PTHR41523; TWO-COMPONENT SYSTEM SENSOR PROTEIN; 1.
DR Pfam; PF07536; HWE_HK; 1.
DR Pfam; PF08447; PAS_3; 1.
DR SMART; SM00911; HWE_HK; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 1.
DR PROSITE; PS50113; PAC; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
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 Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Virulence {ECO:0000256|ARBA:ARBA00023026}.
FT DOMAIN 91..143
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
SQ SEQUENCE 337 AA; 36822 MW; CA17DF3910F1F220 CRC64;
MTKDFKTPLN IPLTFEDMEL GLKVARVGLG KVDYRADTLR CDALAAEFFG LDAGVELPRA
ELHARIHPED WPQVEEGLTC LLSPEHPLQV LDMTHRILLP DGPLRWVNAR KQVTYDAEGV
PVEGVFAIVD ITAREVAEQR AKFLIGELGH RAKNLITVVS GIVRQLARHS PPEEVADRLL
ARLAALSRNQ EAMMHDAGSR FGLRQIFTEQ VKPFAGAARE RVVLNGPDLM ISSNAAQILG
MVTHELATNA AKYGALSDGS GKVEMTWSVE GEERPDFTLS WVERGGPKVT VTAKPGFGTQ
VLTKLTQASL GAKTEVAYDT EGLAFKLRAP LKALSSD
//