ID A0A0K1ECT9_CHOCO Unreviewed; 1775 AA.
AC A0A0K1ECT9;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, 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=CMC5_025390 {ECO:0000313|EMBL:AKT38393.1};
OS Chondromyces crocatus.
OC Bacteria; Myxococcota; Polyangia; Polyangiales; Polyangiaceae;
OC Chondromyces.
OX NCBI_TaxID=52 {ECO:0000313|EMBL:AKT38393.1, ECO:0000313|Proteomes:UP000067626};
RN [1] {ECO:0000313|EMBL:AKT38393.1, ECO:0000313|Proteomes:UP000067626}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Cm c5 {ECO:0000313|EMBL:AKT38393.1,
RC ECO:0000313|Proteomes:UP000067626};
RA Zaburannyi N., Bunk B., Maier J., Overmann J., Mueller R.;
RT "Genome analysis of myxobacterium Chondromyces crocatus Cm c5 reveals a
RT high potential for natural compound synthesis and the genetic basis for the
RT loss of fruiting body formation.";
RL Submitted (JUL-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; CP012159; AKT38393.1; -; Genomic_DNA.
DR RefSeq; WP_050430620.1; NZ_CP012159.1.
DR STRING; 52.CMC5_025390; -.
DR KEGG; ccro:CMC5_025390; -.
DR PATRIC; fig|52.7.peg.2762; -.
DR Proteomes; UP000067626; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd14014; STKc_PknB_like; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.30.450.40; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR041664; AAA_16.
DR InterPro; IPR003018; GAF.
DR InterPro; IPR029016; GAF-like_dom_sf.
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; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR PANTHER; PTHR43642; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE G; 1.
DR PANTHER; PTHR43642:SF1; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE G; 1.
DR Pfam; PF13191; AAA_16; 1.
DR Pfam; PF01590; GAF; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00069; Pkinase; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00065; GAF; 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; SSF55781; GAF domain-like; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000067626}.
FT DOMAIN 6..266
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 1531..1775
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT COILED 1481..1515
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 1775 AA; 195506 MW; 58D09493A6DE2820 CRC64;
MEICGCDVLE RVREGSRTTT YRARRRSDGL AVLLKVLREP TPSQAQLATL RHEETILGEL
DIDGVLRCHG IVEEGGRAAL LLEDFTGSPL DALGVAGSLP IARVVTLAID VVGILEAIHQ
RGVVHRDLTP ATIAMRSGDE TIKFIDFGLA SLLPEHGSTF TSPGGLQGSL AYMAPEQTGR
MNRPIDYRAD YYSLGVTLFE LLTGHLPFTS GDGIELVHAH IARQPPSPRL STPEVPEVLA
AIVLKLMAKS AEGRYQSAQG IRADLARCLE QLQKDGDIAP FSIARRDRPT TFKLPQKLYG
RDADVQTLLT AFEHSLRGVV LMLVSGPSGI GKTSLIREVY RPITVRRGYF IAGKFDQYRH
EDPHAALKQA LRELSDQLLA ESEEHVLEFQ KRARDTLGSH ARILTELCPS LARLLGEHPE
MPTLSHPENL YRFNRAVTGF LASVATPEHP LCVFFDDLQW ANADALKLLE HLSRVEQDLA
LLIIGAHRDE EILDAQALAL ALRAIEARGA RVERVCLSPL GLPELKEMVA DTLSIPREAG
EPLAELLLSR TAGNPFFVRE FFTSLHADGA IEAHDDGYRW SVDRMRAHGV TDNLVDLMTA
RLRQLCPETR ELLLFAACLG SVFELGTLAL VSGRSIDEVS HTSWPAVIEG LIFLVPQSAS
VAQMIEVGPL LKGRFAHDRI QQATLSMVGA KARARLARTI GRQLAQAEGS EGQSHRLLDI
VGLLNEGRIA IDDRHELLDL AALNLRAARK ARDNAAAQQA LSYGRAGILL IEEGDWSDHY
ELTRDLYMTA LEAAIACGDI EAARELSEVA RPRLQGLLDE VRQLSLDGQV LFSQQRVTEA
LRTYLAALAR LGCELPQDPT PEEVEREIQR NLRSLKAHSV EELEGLSECR NPVDCTAMFL
LSQIISSSGT GGASVYPIAV CQLVAMSLRC GVGRHTSFGY ALFGSLLLAR NEIDEACRLG
HVALRIADRS ANCEFRSQTY YVAGYHLVHV ERHLRDLAEM LSNTHRFALE AGSLFFSAAA
AQGLCLARFL SGEDLSPLLA DMEGYARLCE RLQQPMVCDW LRLYIQVSLN LIGKTGDLTM
LRGPAYVEAE RVPHQRATGD AGGMSHYHFC KMLLHYLFGE HDHAAASADT LASYPVGSEH
SLAATFIAFI QSLSYLALYE RAENGDRERK LGFVAQSLVK IEQWCKHHPP NYEHKLLLIS
AERARVLGDH EAARAAFTRG TELADRSGYR HEAAIGHELA GRFYILRGEH KLARKHLRDA
HEGFLRWGAV TKARQLEREY PGVVPLVAAG MSSGSTATET GGRELDFDVL DLVSVLNASQ
DLSREIELDR LLARLMQILL ETSGATVGYL LMEQGKKWVI EGEKAVTQEN AIVLKSIPVA
ELMARGHRGL PASIIHYVAR SQESLVVDDA SADPRFSGDP CTIRNAIGSV LCFPLGRPGG
RRGLVYLENS LLKGAFTPAR IRILQMLSTQ AVISIENAAL YNTLEQRVES RTSELRKKNE
ELATALTHLR ETQDRMFVQE RLASLGSLAA GIAHELRNPL NFVNNFARFA AALVDEIHDG
LLPSGRVSSA GRFARLDEAL EDLKVNVTKI GEHGRRMDGI IRSMLDHSRD DRGARQWVDL
NTLVETYVNI GYQGSRARTS TGEIAIEMTL DPSIGLVSIV PQEVSRVIIN LVDNACYAVT
QRAGECPLGF EPRIEVITRN EEDCCEIRIR DNGSGVPRDI RARIFDPFFT TKPPGEGTGL
GLSICHTIVT EGNGGLLRCE SEEGIFAEFI VRLPK
//
