ID K9WJJ5_9CYAN Unreviewed; 1815 AA.
AC K9WJJ5;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 58.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=Mic7113_4293 {ECO:0000313|EMBL:AFZ19991.1};
OS Allocoleopsis franciscana PCC 7113.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Coleofasciculales;
OC Coleofasciculaceae; Allocoleopsis; Allocoleopsis franciscana.
OX NCBI_TaxID=1173027 {ECO:0000313|EMBL:AFZ19991.1, ECO:0000313|Proteomes:UP000010471};
RN [1] {ECO:0000313|EMBL:AFZ19991.1, ECO:0000313|Proteomes:UP000010471}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 7113 {ECO:0000313|EMBL:AFZ19991.1,
RC ECO:0000313|Proteomes:UP000010471};
RG US DOE Joint Genome Institute;
RA Gugger M., Coursin T., Rippka R., Tandeau De Marsac N., Huntemann M.,
RA Wei C.-L., Han J., Detter J.C., Han C., Tapia R., Chen A., Kyrpides N.,
RA Mavromatis K., Markowitz V., Szeto E., Ivanova N., Pagani I., Pati A.,
RA Goodwin L., Nordberg H.P., Cantor M.N., Hua S.X., Woyke T., Kerfeld C.A.;
RT "Finished chromosome of genome of Microcoleus sp. PCC 7113.";
RL Submitted (JUN-2012) 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; CP003630; AFZ19991.1; -; Genomic_DNA.
DR STRING; 1173027.Mic7113_4293; -.
DR KEGG; mic:Mic7113_4293; -.
DR PATRIC; fig|1173027.3.peg.4744; -.
DR eggNOG; COG0745; Bacteria.
DR eggNOG; COG0784; Bacteria.
DR eggNOG; COG2205; Bacteria.
DR eggNOG; COG2461; Bacteria.
DR eggNOG; COG5000; Bacteria.
DR eggNOG; COG5002; Bacteria.
DR HOGENOM; CLU_000445_82_0_3; -.
DR Proteomes; UP000010471; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd16922; HATPase_EvgS-ArcB-TorS-like; 2.
DR CDD; cd00082; HisKA; 2.
DR CDD; cd00130; PAS; 5.
DR CDD; cd17580; REC_2_DhkD-like; 1.
DR CDD; cd17574; REC_OmpR; 1.
DR Gene3D; 1.10.287.130; -; 2.
DR Gene3D; 3.30.450.40; -; 1.
DR Gene3D; 3.40.50.2300; -; 2.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 2.
DR Gene3D; 3.30.450.20; PAS domain; 6.
DR InterPro; IPR011006; CheY-like_superfamily.
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; IPR001610; PAC.
DR InterPro; IPR000014; PAS.
DR InterPro; IPR000700; PAS-assoc_C.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR013656; PAS_4.
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; 5.
DR PANTHER; PTHR43547:SF2; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE C; 1.
DR PANTHER; PTHR43547; TWO-COMPONENT HISTIDINE KINASE; 1.
DR Pfam; PF13185; GAF_2; 1.
DR Pfam; PF02518; HATPase_c; 2.
DR Pfam; PF00512; HisKA; 2.
DR Pfam; PF08447; PAS_3; 1.
DR Pfam; PF08448; PAS_4; 3.
DR Pfam; PF13426; PAS_9; 1.
DR Pfam; PF00072; Response_reg; 2.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 2.
DR SMART; SM00388; HisKA; 2.
DR SMART; SM00086; PAC; 4.
DR SMART; SM00091; PAS; 6.
DR SMART; SM00448; REC; 2.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 2.
DR SUPFAM; SSF52172; CheY-like; 2.
DR SUPFAM; SSF55781; GAF domain-like; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 2.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 6.
DR PROSITE; PS50109; HIS_KIN; 2.
DR PROSITE; PS50113; PAC; 4.
DR PROSITE; PS50112; PAS; 5.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 2.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000010471};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 356..573
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 637..753
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 776..846
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 893..963
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 965..1017
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 1018..1088
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 1091..1143
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 1158..1243
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 1241..1293
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 1302..1366
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 1364..1422
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 1454..1672
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 1694..1812
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT COILED 323..350
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 746..790
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1129..1161
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 686
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 1743
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1815 AA; 202541 MW; 8A489B980B4A4F1C CRC64;
MTQQGEEIAL EQLFAGGGET GAMMRSLDWS RHPLGSVDQW PQSLKTMVRI MLTSRQPMFV
WWGEQLINLY NDAYKSIVGG KHPKALGQPA SEVWREIWDQ VGPRAESAML KNEGTYDEAL
LLIMERNGYP EETYYTFSYS PVPNDQGGTG GIICANTDDT QRIIGERQLS LLRELAAKTA
DARTFDDACT RSAKCLETNP YDLPFAMIYL VDPGQKCVVL TGTSGIDRTH AAVPETIALD
SDSPWPFAEA IAMHKPCLVA DLEALFGNLP MGAWQRPPHQ AVVVPIAPSG QTGQAGILIV
GLNPFRLFDD NYRGFIDLVA AQIAASIANA QAYEEERKRA EALAELDRAK TIFFSNISHE
FRTPLTLMLG PLEEMLANSA RLLPSERSHL ETAHRNSLRL LKLVNTLLDF SRIEAGRVQA
VYEPTDLAMF TADLAGMFRC AIEQAGMRLC VECPPLPEPV YVDREMWEKI VLNLLSNAFK
FTWEGEITVA LGWANDHVEL EVRDTGTGIP AEEMPHLFER FHRVEGARGR TYEGSGIGLS
LVQELVKLHG GTIQVSSVVD RGSCFTVVIP TGYAHIPKER ISTPRTLAST AIGAATYVEE
ALRWLPEGAG EPGSRGAGEP GREVYPVSLN SCVPSAHILL ADDNADMRDY VKRLLVTQGY
EVETVGDGIA ALARIHERTP DLVLTDVMMP RLDGLGLLRS LRDDPRTREI PIILLSARAG
EKSRIEGLEA GADDYLIKPF SARELLARVE ASLKLAQMRQ EAASREEVLR AEVQSAKDTL
ENVLSRIRDQ FLALDQDWRY TYTNDRVVEV TGKSREELLG KSIWELYPDT IGSQFQIEVQ
RAVAEQIPIQ FEYFYPSLNR WFENRIYPSA DGLSVFVADI TNRKQAEEAL QQREAELQLI
TDTVPALIAY VDRDCRYRFA NRAFTRWFGK LVEEIIGQRV EEFVGETAYQ YIRSDIEKAL
TGESVTSELW VPFRDGGSRY VRRQYIPDID AQGEVRGFFA MITDLTDLKR TQEAFRASEE
RFSVIVNQAT VGIAQMDLTA QFVLVNQKYC DIVGYPMAEL LHKRKQDITH PEDLPYNMEL
FHRLVTRGES YALEKRYIRK DGSEVWVSNY VAAICDASGK PESAISVVLD ISEQKAALRE
RQQAEAERER LLQELAIERA RFEAVLRQMP AGVMIADAAS GKLVLTNEQA KQIVGYDYEQ
SIQLAEYNQI VPFEGFRSDG QLYNPEDYPL MRSLQTGETI TNEEIELQRG DGSHIVMNAN
SAPILDSKGQ IIAAVVVFQD ITERKRAEEA LRQALLKLNF HVENTPMAVV EWDRDFRIIR
WSAAAERILG WKAEEVIGKQ LTELRFVYEE DAEAVAEVCR RLVYSEEPHI VGYNRNYTKD
GDIVHCEWYN SSLRDELGRM TSVLSLVLDV TERKRAEQER EQLLKREQAA RAESEAARSA
AETANRIKDE FLAVLSHELR SPLNPILGWS RLLQTRKFDA AKTAEALATI ERNAKLQAEL
IEDLLDVSRI LRGKLSLNIT SVALTSTIQA AMETVRLAAE AKSIQMSTKL EPQVGKVSGD
ASRLQQVVWN LLSNAIKFTP PGGRVDIQLE RIDSYAQIVV SDTGKGIPVD FLPHVFDYFR
QADATTTRKF GGLGLGLAIV RHLVELHGGT VQADSAGEGQ GATFTVRLPL LLSPPQSDQD
SEQPEPSLDL QGIEILVVDD DIDTREFVAF LLEQYGAQVT AVGTAGEALA ALSQSVPDVL
LSDIGMPEMD GYMLMQKVRT LPPEQGGQIP AIALTAYAGE INYQQALSAG FQSHLSKPVE
PAELVALVTK LAQRQ
//
