ID A0A127V8K0_9SPHI Unreviewed; 925 AA.
AC A0A127V8K0;
DT 11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT 11-MAY-2016, sequence version 1.
DT 24-JAN-2024, entry version 36.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=AY601_0574 {ECO:0000313|EMBL:AMP97527.1};
OS Pedobacter cryoconitis.
OC Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC Sphingobacteriaceae; Pedobacter.
OX NCBI_TaxID=188932 {ECO:0000313|EMBL:AMP97527.1, ECO:0000313|Proteomes:UP000071561};
RN [1] {ECO:0000313|EMBL:AMP97527.1, ECO:0000313|Proteomes:UP000071561}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PAMC 27485 {ECO:0000313|EMBL:AMP97527.1,
RC ECO:0000313|Proteomes:UP000071561};
RA Lee J., Kim O.-S.;
RT "Complete genome sequence of Pedobacter cryoconitis PAMC 27485.";
RL Submitted (MAR-2016) 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; CP014504; AMP97527.1; -; Genomic_DNA.
DR RefSeq; WP_068396140.1; NZ_CP014504.1.
DR AlphaFoldDB; A0A127V8K0; -.
DR KEGG; pcm:AY601_0574; -.
DR PATRIC; fig|188932.3.peg.589; -.
DR OrthoDB; 9809670at2; -.
DR Proteomes; UP000071561; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:InterPro.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR GO; GO:0043565; F:sequence-specific DNA binding; IEA:InterPro.
DR CDD; cd00075; HATPase; 1.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd06308; PBP1_sensor_kinase-like; 1.
DR CDD; cd17574; REC_OmpR; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.40.50.2300; -; 3.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 1.10.10.60; Homeodomain-like; 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; IPR009057; Homeobox-like_sf.
DR InterPro; IPR018060; HTH_AraC.
DR InterPro; IPR028082; Peripla_BP_I.
DR InterPro; IPR025997; SBP_2_dom.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR PANTHER; PTHR43547:SF2; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE C; 1.
DR PANTHER; PTHR43547; TWO-COMPONENT HISTIDINE KINASE; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF12833; HTH_18; 1.
DR Pfam; PF13407; Peripla_BP_4; 1.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00342; HTH_ARAC; 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; SSF46689; Homeodomain-like; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR SUPFAM; SSF53822; Periplasmic binding protein-like I; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS01124; HTH_ARAC_FAMILY_2; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Kinase {ECO:0000313|EMBL:AMP97527.1}; Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000071561};
KW Transferase {ECO:0000313|EMBL:AMP97527.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 345..368
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 412..626
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 674..789
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 821..920
FT /note="HTH araC/xylS-type"
FT /evidence="ECO:0000259|PROSITE:PS01124"
FT MOD_RES 722
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 925 AA; 104974 MW; D53E8AF534ED7051 CRC64;
MVQKHLLLAR IFILVLLSAL LLSCGKKKKK DPEYVIAFSQ CVGSDLWRRT MLEEMKMELS
LHPDAKLIYR DANNSSERQV KQVKEMLDQG IDLLIISPNE ANPLTPIVEQ AYNKGIPVVI
IDRKISSSSY TAYVGADNYQ IGKMAGEYVG SLLAGKGNII EIMGLPGSSP AIERQKGFSK
GLERFKGIKI SAQIYGDWLK PNSEKQLLKF KEALTYTDLI FAHNDQMASG AKEVLQQLGL
TKRIKIIGID ALPGAGGGLQ MIDSKVINAS MLYPTGGKEA ISTAFKILGK ASFDKENILP
SLVIDSSNVQ LMKMQWNKFS SQQQDIERQQ TLLEEQRSLF DNQQFILNII VIALVLSFVF
GGLAFFSLQE NRKINKKLEA NNLEILNQRN QLIEMSEKAK TATEAKLNFF TNISHEFRTP
LTLILSPLED LIKNEKINAL AGQNLKLIHK NVFRLLRLIN QLIEYRKIEL DKMRIKASAN
KLTDFVNEIL ESFQHSAKKR NIDLRLISTE KDIVVWFDAN MLDKVIFNLL SNALKFTTAN
GTIHLTIKRQ DRFIAIEVKD NGTGMEPEEV NHIFEHFYQA ESNVARGSGL GLSLSKELMK
LHHGDLIVES KKWYGTTFTI KLLTGEDHFS VKEKSVEPLL KEELHENAKI YTTDLEEHRE
QKSSDALRQL KEQSILIIED NSDLLYYLGD KFDDEYEIFI ANTGESGITS AYEQVPDLII
CDVVLPDLSG RQISEKLKSD VRTSHIPIIL LTAQDSLEQQ INGIESMADA YIIKPFNYNY
LLANVRNLLK NRLLLKSHYT SDISSIAKQP ISKSLDKKFI NDFSGLVEQN LGNENFSVEQ
ISKTLGVSRV QLYRKIKALL DCSVNDYILN RRLKKARYLL TNERYSIAEI TYMVGFSSPN
YFSTVFKSKY GMRPSEFKRN QTTNP
//
