ID I6Z437_MELRP Unreviewed; 1118 AA.
AC I6Z437;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2012, 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=MROS_0652 {ECO:0000313|EMBL:AFN73895.1};
OS Melioribacter roseus (strain JCM 17771 / P3M-2).
OC Bacteria; Ignavibacteriota; Ignavibacteria; Ignavibacteriales;
OC Melioribacteraceae; Melioribacter.
OX NCBI_TaxID=1191523 {ECO:0000313|EMBL:AFN73895.1, ECO:0000313|Proteomes:UP000009011};
RN [1] {ECO:0000313|EMBL:AFN73895.1, ECO:0000313|Proteomes:UP000009011}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 17771 / P3M-2 {ECO:0000313|Proteomes:UP000009011};
RX PubMed=23301019; DOI=10.1371/journal.pone.0053047;
RA Kadnikov V.V., Mardanov A.V., Podosokorskaya O.A., Gavrilov S.N.,
RA Kublanov I.V., Beletsky A.V., Bonch-Osmolovskaya E.A., Ravin N.V.;
RT "Genomic analysis of Melioribacter roseus, facultatively anaerobic
RT organotrophic bacterium representing a novel deep lineage within
RT Bacteriodetes/Chlorobi group.";
RL PLoS ONE 8:E53047-E53047(2013).
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; CP003557; AFN73895.1; -; Genomic_DNA.
DR RefSeq; WP_014855332.1; NC_018178.1.
DR AlphaFoldDB; I6Z437; -.
DR STRING; 1191523.MROS_0652; -.
DR GeneID; 78565667; -.
DR KEGG; mro:MROS_0652; -.
DR PATRIC; fig|1191523.3.peg.681; -.
DR eggNOG; COG0784; Bacteria.
DR eggNOG; COG2202; Bacteria.
DR eggNOG; COG2205; Bacteria.
DR HOGENOM; CLU_280724_0_0_10; -.
DR OrthoDB; 9811889at2; -.
DR Proteomes; UP000009011; Chromosome.
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; 4.
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; 3.30.450.20; PAS domain; 5.
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; IPR001610; PAC.
DR InterPro; IPR000014; PAS.
DR InterPro; IPR000700; PAS-assoc_C.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR013767; PAS_fold.
DR InterPro; IPR013655; PAS_fold_3.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR NCBIfam; TIGR00229; sensory_box; 4.
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; PF00989; PAS; 3.
DR Pfam; PF08447; PAS_3; 1.
DR Pfam; PF13188; PAS_8; 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; 3.
DR SMART; SM00091; PAS; 5.
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 SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 5.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50113; PAC; 2.
DR PROSITE; PS50112; PAS; 3.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Kinase {ECO:0000313|EMBL:AFN73895.1};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000009011};
KW Transferase {ECO:0000313|EMBL:AFN73895.1}.
FT DOMAIN 254..324
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 377..430
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 449..501
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 623..698
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 703..755
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 773..992
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 994..1112
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT MOD_RES 1045
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1118 AA; 128298 MW; 9F9A3EDB6B57D160 CRC64;
MTDYSADKYT SGGKMLKLRA MFEAAPVGIL IFSNEFKVRF VNQTFFGFKG IAPLESTDIT
GENIEKIGLF EDKEIFSLLK ENQPFEKELY SSVTASGDRM AVLIKYVPVN TERQFEGGIV
VLEDIKYRFS GEGNESLNYK KVFESICDCY LICDREGNIN YSSKECWRYN FLFDSATLKE
EKPGRLSGIL FKKLFEQLEK SNATLWTEIP YVKDDKQQIA VIALIPLNGN VLLLVRNKEI
DKKEKELLQE EIKELRKYEY IISNMIDAVF LADDFNRIVY WSESAARLFG LKRSEVHGKE
VSGLFSKIDR NYLHSISQKL IENKYVEDFI KLGDDEENAE YFTLRIGKLK EGVKEYFVFI
CADSTFRIRK ELELKKSEER FRKIVTHTQE FICILDLNGK IQYANPAMLQ SFGYTDQEIS
SLYFVDLVEP YYLMTNGFSL SDLEERKTET IELPLITKHD QKIYVHASFS TVYDDRGMPL
YYNVFLTDIS MLKEAEKDLM LIRSIFEASH DGIALINRRK LFLVNEAFVK MFGYKSASEI
IGKDPLDFVD VDDIIKVGRN IQSLEEGRES PSRFEFKGIK ADEIPIELES SVSSYEAEGE
KFIVWSLRDI TPQKKALEAL RLSEERYRSI TENIDESFWT AEKIRGKLVQ VFYTPAIEKI
TGYKPEKFLE DRFLWKKIIH PDDLANVIEN LKRLYRFSDK NYEKLEYRII DSLGNIIWIE
NKISVRRDDS GRIVKIFGIV NDITMSKRAQ DELKRSAAEL KELNETKDRF ISIISHDLRT
PFSSILGFTD FLLNEKDLTE EKRTQYIRFI EESARNMLEL VNSLLDWTRL QTGRIKFEPN
RINVKQAVDK SIQILSGAAL RKGIDLKSEL SDNLFIHADE NLLLQAINNL VSNAIKFTPT
GGAITISAAP DVKNKSVVFS VKDTGTGIKE EDIPKLFKVD TKFTTPGTAG EKGSGLGLSL
VREIILKHGG DIHVKSQYGK GSEFIFTVPV SSTTILLVDD IKTDRILYSK LIRNLIEGYT
ITEAENGKEA IEIVKSASPA LIISDHNMPV MNGYDFVKQL TLSDLKFKPP VIILSSDINP
SVEEQYKELG VEFVFRKPVN LATFKNAIEK SLRKAFFG
//
