ID G2IVH2_PSEUL Unreviewed; 702 AA.
AC G2IVH2;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 67.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN OrderedLocusNames=NH8B_0289 {ECO:0000313|EMBL:BAK75138.1};
OS Pseudogulbenkiania sp. (strain NH8B).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Neisseriales;
OC Chromobacteriaceae; Pseudogulbenkiania.
OX NCBI_TaxID=748280 {ECO:0000313|EMBL:BAK75138.1, ECO:0000313|Proteomes:UP000001274};
RN [1] {ECO:0000313|Proteomes:UP000001274}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NH8B {ECO:0000313|Proteomes:UP000001274};
RX PubMed=22038961; DOI=10.1128/JB.06127-11;
RA Ishii S., Tago T., Nishizawa T., Oshima K., Hattori M., Senoo K.;
RT "Complete genome sequence of the denitrifying and N(2)O-reducing bacterium
RT Pseudogulbenkiania sp. strain NH8B.";
RL J. Bacteriol. 193:6395-6396(2011).
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}.
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DR EMBL; AP012224; BAK75138.1; -; Genomic_DNA.
DR RefSeq; WP_014085717.1; NC_016002.1.
DR AlphaFoldDB; G2IVH2; -.
DR STRING; 748280.NH8B_0289; -.
DR KEGG; pse:NH8B_0289; -.
DR eggNOG; COG5000; Bacteria.
DR HOGENOM; CLU_019564_0_0_4; -.
DR OrthoDB; 9815750at2; -.
DR Proteomes; UP000001274; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd06225; HAMP; 1.
DR CDD; cd00082; HisKA; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 6.10.340.10; -; 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; IPR003660; HAMP_dom.
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; IPR017232; NtrY.
DR InterPro; IPR045671; NtrY-like_N.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR013656; PAS_4.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR PANTHER; PTHR43065:SF10; PEROXIDE STRESS-ACTIVATED HISTIDINE KINASE MAK3; 1.
DR PANTHER; PTHR43065; SENSOR HISTIDINE KINASE; 1.
DR Pfam; PF00672; HAMP; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF19312; NtrY_N; 1.
DR Pfam; PF08448; PAS_4; 1.
DR PIRSF; PIRSF037532; STHK_NtrY; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00304; HAMP; 1.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF158472; HAMP domain-like; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 1.
DR PROSITE; PS50885; HAMP; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
PE 4: Predicted;
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:BAK75138.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000001274};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 32..55
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 75..94
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 271..294
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 296..348
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 491..701
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
SQ SEQUENCE 702 AA; 77951 MW; 5DEFE409B9803904 CRC64;
MRYAMIAMAT FAAILLYLLA LATGNTSKLA EYYWWVFGIN ALLLVALLGV VGRQLVRLRR
RVKGRVFGAK LTQRLVMMFA VVALVPGLLV YTISTQFLSR SIESWFDVRV ESALDRGLEL
GRNALGYVLQ DVGRKARVVQ DDIDALPDSG LPARLERLRE QLGLNEVAIF NRQGQLLAFA
SGDLAGLPQT PSREALRTLR PRQPVQTIEN DRRNQLALKV LMAYHDRHDE TRVMQVIQAA
PESIAHDAEL IDTARADYRQ LLLSRDGLRT FYTLTLTLAC LLALTAALAF ALWLSERLSA
PLSELAAGTR AVAQGDFSKR HPVYRRDELG ILTTMFNRMT QQLDEARQLA DENRLKLESG
KLYLESILVN LRAGVMAFDD GWRLRAANTS ASRILGVDFA ELAEAPFREW TRLVPALVPL
VDNVCEHADS ERQPEWQTQL DYTTAQGERI LLVRGARLPE GSGSGYVVVF DDITELARAQ
RDAAWGEVAK RLAHEIRNPL TPIQLAAERL AMKLADKLEG SDADLLRRAT DTIVKQVSAL
KSMVDAFRDY ARSPRIKLVA LDLNQLVREV MTLYESNAAV KMTLSEQPLM IMGDAALLRQ
VLHNLLQNAQ DAVLDVDIPM IHISSRQEGR SAIVCVQDNG AGFPADILPR AFEPYVTNKP
KGTGLGLAVV KKIIEEHHGQ IALGNAGQQG ARILLTLPLL EA
//
