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Database: UniProt
Entry: A0A0T5NRT1_9RHOB
LinkDB: A0A0T5NRT1_9RHOB
Original site: A0A0T5NRT1_9RHOB 
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}.
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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
//
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