ID A0A0N7HIG6_9RHOB Unreviewed; 839 AA.
AC A0A0N7HIG6;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=IMCC12053_1217 {ECO:0000313|EMBL:ALI55165.1};
OS Celeribacter marinus.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Celeribacter.
OX NCBI_TaxID=1397108 {ECO:0000313|EMBL:ALI55165.1, ECO:0000313|Proteomes:UP000064920};
RN [1] {ECO:0000313|EMBL:ALI55165.1, ECO:0000313|Proteomes:UP000064920}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IMCC 12053 {ECO:0000313|EMBL:ALI55165.1,
RC ECO:0000313|Proteomes:UP000064920};
RA Wang D.B., Wang M.;
RL Submitted (MAY-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 -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR EMBL; CP012023; ALI55165.1; -; Genomic_DNA.
DR RefSeq; WP_062216644.1; NZ_FOSM01000001.1.
DR AlphaFoldDB; A0A0N7HIG6; -.
DR STRING; 1397108.IMCC12053_1217; -.
DR KEGG; cmar:IMCC12053_1217; -.
DR PATRIC; fig|1397108.4.peg.1246; -.
DR OrthoDB; 9801651at2; -.
DR Proteomes; UP000064920; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd00130; PAS; 1.
DR CDD; cd17546; REC_hyHK_CKI1_RcsC-like; 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 Gene3D; 1.20.120.160; HPT domain; 1.
DR Gene3D; 3.30.450.20; PAS 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; IPR036641; HPT_dom_sf.
DR InterPro; IPR001610; PAC.
DR InterPro; IPR000014; PAS.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR013767; PAS_fold.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR008207; Sig_transdc_His_kin_Hpt_dom.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
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; PF00989; PAS; 1.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00086; PAC; 1.
DR SMART; SM00091; PAS; 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; SSF47226; Histidine-containing phosphotransfer domain, HPT domain; 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; PS50894; HPT; 1.
DR PROSITE; PS50112; PAS; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Kinase {ECO:0000313|EMBL:ALI55165.1}; Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000064920};
KW Transferase {ECO:0000313|EMBL:ALI55165.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 168..193
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 206..277
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 353..571
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 598..715
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 743..839
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT MOD_RES 647
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 782
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
SQ SEQUENCE 839 AA; 90822 MW; B01B4E41C5884485 CRC64;
MALLLFFVVS MSIWEIARYG GAVRTEIESL AIANSDSQQW SLAQLEVEFD QMRIALLMFD
PDDPVRVREF SQRFDVFYSR VETVMNGDAF GRVFDGSSVL SRMGSLREFT VSTAKIVDAG
PQAVADAHPP LSSQMADLAL NVRAISLQGI REFAVAAQDQ RERVYSSLVR LAAVAGVLVT
ALSMGLFGLW YLWQFGARQT RSLRSAKLRF EAVINTALDA VVVVDQDARV VEFNPAATTI
FGYSTQEAIG RSLSELIVPD HLVEAHEAGF KRYRDGGTAR VVGKGLISME AKRKNGELFP
VELSISSIRL GNRELFVSYM RDITRRVEAE NDLISARDQA MQSERAKAAF VAVMSHEIRT
PLNGLLGTLE NLKVTHLTGG QKRYVQAMEY SGAILLGHVN DVLDVEKLEA GKFDFARVAL
SPYELANRIV ETVAADAQER GNRVLVEAVG DVPGFIVGDP ARILQILMNL VGNANRFTED
GSVTIEIEFH NAASQIEYRV IDTGVGIPEG DVDRVFEDFV TISADNARSG SGTGLGLGIA
RRVVRAMGGQ IGVESEVGEG SVFWFSIPAD TAASIDAGPV EAESGSVAPT PRSQAPLRIL
VVEDNAINRD VLCEMLMRGG HSFEAVVDGA QAVRAASSSV FDVILMDLNM PVLNGTDATR
IIREGDGPNA TAPIIAVTAN TAKDITERLR AEGFSDVIIK PITKRKLDEV MQISVRPGSA
LSDAASGVIV NEEILSDLGE ALGADRLRHT CERFVDEGYQ LIAEMRAMIG QRDVAGYAKV
AHKFAGSAAL VGANALMELL LIQEQQAHTR TLAALTVDLS RLEGVFAQTC DALEARLAA
//
