ID W3RH15_9BRAD Unreviewed; 603 AA.
AC W3RH15;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 46.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=X566_15745 {ECO:0000313|EMBL:ETR76037.1};
OS Afipia sp. P52-10.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Nitrobacteraceae; Afipia.
OX NCBI_TaxID=1429916 {ECO:0000313|EMBL:ETR76037.1, ECO:0000313|Proteomes:UP000018975};
RN [1] {ECO:0000313|Proteomes:UP000018975}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=P52-10 {ECO:0000313|Proteomes:UP000018975};
RX PubMed=25874801;
RA Pickering B.S., Tyler S., Smith G., Burton L., Li M., Dallaire A.,
RA Weingartl H.;
RT "Identification of a novel afipia species isolated from an Indian flying
RT fox.";
RL PLoS ONE 10:E0121274-E0121274(2015).
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 -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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:ETR76037.1}.
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DR EMBL; AZSJ01000004; ETR76037.1; -; Genomic_DNA.
DR AlphaFoldDB; W3RH15; -.
DR STRING; 1429916.X566_15745; -.
DR PATRIC; fig|1429916.3.peg.3193; -.
DR eggNOG; COG2205; Bacteria.
DR Proteomes; UP000018975; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd16922; HATPase_EvgS-ArcB-TorS-like; 1.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd00130; PAS; 1.
DR Gene3D; 1.10.287.130; -; 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; 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; IPR004358; Sig_transdc_His_kin-like_C.
DR NCBIfam; TIGR00229; sensory_box; 1.
DR PANTHER; PTHR43047:SF79; HISTIDINE KINASE; 1.
DR PANTHER; PTHR43047; TWO-COMPONENT HISTIDINE PROTEIN KINASE; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF08448; PAS_4; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00091; PAS; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50113; PAC; 1.
DR PROSITE; PS50112; PAS; 1.
PE 4: Predicted;
KW Kinase {ECO:0000313|EMBL:ETR76037.1}; Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000018975};
KW Transferase {ECO:0000313|EMBL:ETR76037.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 31..53
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 59..78
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 90..120
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 132..156
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 168..187
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 202..272
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 275..335
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 353..573
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
SQ SEQUENCE 603 AA; 65411 MW; 19A3EF8A2B28A94E CRC64;
MTAILSIRRF LDALLHPSAR YDAMMAERHR VFIGTRLLGG FVLLASFPIY LAVRGAPGLL
EVACFAWLTV PILLAYYLSR TGRYEDAHCL SSVLLAGVVM LVAINTGGIA SFAAVWLVAI
PIEAALSGSR RIVAGATALS LMCVLLLIGA STGDFLPASK IPQQLNSVFE AIGIASVVLC
CATLAFMTEM LGSTSRGLLS AEERRYSLLA RNMSDVISLH RRNGAIEFIS PAAQALFGTQ
LGQLAGHGLF DRVHVADRPA YLTAIAEVAR GAGDRDVEFR VRCGADEQVG PSFIWVEMRC
RPLERNADIS GPDAEVVAVL RDITERKAQE QALEDARREA ERAHAAKSQF LSTMSHELRT
PLNAIIGFSE MMVREAELNL DAERRREYAQ LINDSGQHLL SVVNGILDMS KIESGGFEIS
AEPFVPREAI VSCSNLMALK AREGGLDLVV NVPENLPDMV GDRRAFKQIL LNLLSNAIKF
TERGGSVTVS ASVEGANLAL RVEDTGVGIA PDDMKRLGDP FFQAEKTYRR RHEGTGLGLS
IVKALVAMHH GEMNVQSKVD VGTTISVKLP LDLDKVVPKP SPVVTTLMPK SKEQSEQRIK
RSA
//
