ID A0A0B6WWZ8_9BACT Unreviewed; 635 AA.
AC A0A0B6WWZ8;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=PYK22_01581 {ECO:0000313|EMBL:CDM65576.1};
OS Pyrinomonas methylaliphatogenes.
OC Bacteria; Acidobacteriota; Blastocatellia; Blastocatellales;
OC Pyrinomonadaceae; Pyrinomonas.
OX NCBI_TaxID=454194 {ECO:0000313|EMBL:CDM65576.1, ECO:0000313|Proteomes:UP000031518};
RN [1] {ECO:0000313|EMBL:CDM65576.1, ECO:0000313|Proteomes:UP000031518}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K22 {ECO:0000313|EMBL:CDM65576.1,
RC ECO:0000313|Proteomes:UP000031518};
RA Stott M.;
RL Submitted (DEC-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:CDM65576.1, ECO:0000313|Proteomes:UP000031518}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K22 {ECO:0000313|EMBL:CDM65576.1,
RC ECO:0000313|Proteomes:UP000031518};
RA Lee K.C.Y., Power J.F., Dunfield P.F., Morgan X.C., Huttenhower C.,
RA Stott M.B.;
RT "Complete genome sequence of Pyrinomonas methylaliphatogenes type strain
RT K22T.";
RL Submitted (JAN-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};
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DR EMBL; CBXV010000005; CDM65576.1; -; Genomic_DNA.
DR RefSeq; WP_060635460.1; NZ_CBXV010000005.1.
DR AlphaFoldDB; A0A0B6WWZ8; -.
DR STRING; 454194.PYK22_01581; -.
DR OrthoDB; 9815750at2; -.
DR Proteomes; UP000031518; 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; cd00082; HisKA; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.40.50.2300; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR InterPro; IPR011006; CheY-like_superfamily.
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; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR PANTHER; PTHR43047:SF72; OSMOSENSING HISTIDINE PROTEIN KINASE SLN1; 1.
DR PANTHER; PTHR43047; TWO-COMPONENT HISTIDINE PROTEIN KINASE; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00448; REC; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF52172; CheY-like; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils}; Kinase {ECO:0000313|EMBL:CDM65576.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000031518};
KW Transferase {ECO:0000313|EMBL:CDM65576.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 18..37
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 44..64
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 76..96
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 108..130
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 150..174
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 186..206
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 212..231
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 277..490
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 510..624
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT COILED 238..268
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 559
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 635 AA; 70167 MW; B2E7FB30A3777736 CRC64;
MQSAGDQSAK GISLKKPFIG AVIAFGVGVL LFSAWHLQVE RLDARFLIIL IITLAFSSRL
VVRIPTIPSQ ISVSDTLIFL TLLLYGREAA VLLSILEASV SSPRFSKRAV TTLFNAAVMG
ISTFLTASAL GRLFGPPERI IYVSYSANLI FALGVMALVQ YITNSGLVAV ASALRTGQAI
WSTWRNYYLW TSVTYLAGAS AAIIVAKLTL LWGFYSVLAT TPIILVVYLT YRTYAQNLEA
ARRHVEELSR YIAEQEKLRA QCAQLEKLSA LGELASGVAH DFNNILSGIL GRAQLLLRTD
DAETIRHGLA IIVKMAEDGA KTVKRIQDFA RQRRHHERKP VSVDQILWDA FEITRPRWKD
DAEAKGAHIQ FDLEPRSFAT VLGDESELRE VLINMIFNAV DALPHGGRIR LASETLGEEV
IISLSDTGIG IGPEIISRIF DPFFTTKEHS GLGLGLAISY SIIQRHGGRI TVESEPGRGT
TFRINLPIAR FSAQTAGPEA VARASAEKAH ILVVDDEDYV RELLCDILSS EGHMVTQAES
ARRALELFER YRFDAVFTDI GMPEMNGWEL ARRVRAIDDE IPIALVTGWG EMIGEEEREK
EGIDWVVAKP FQVDQILDLA SQALERRAKD TQTVG
//
