ID K9V5A3_9CYAN Unreviewed; 1547 AA.
AC K9V5A3;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, 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 ORFNames=Cal6303_4096 {ECO:0000313|EMBL:AFZ03011.1};
OS Calothrix sp. PCC 6303.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Calotrichaceae;
OC Calothrix.
OX NCBI_TaxID=1170562 {ECO:0000313|EMBL:AFZ03011.1, ECO:0000313|Proteomes:UP000010477};
RN [1] {ECO:0000313|EMBL:AFZ03011.1, ECO:0000313|Proteomes:UP000010477}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 6303 {ECO:0000313|EMBL:AFZ03011.1,
RC ECO:0000313|Proteomes:UP000010477};
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 Calothrix sp. PCC 6303.";
RL Submitted (MAY-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};
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000256|ARBA:ARBA00004429}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004429}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the phytochrome
CC family. {ECO:0000256|ARBA:ARBA00006402}.
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DR EMBL; CP003610; AFZ03011.1; -; Genomic_DNA.
DR STRING; 1170562.Cal6303_4096; -.
DR KEGG; calt:Cal6303_4096; -.
DR PATRIC; fig|1170562.3.peg.4465; -.
DR eggNOG; COG0745; Bacteria.
DR eggNOG; COG2203; Bacteria.
DR eggNOG; COG2205; Bacteria.
DR HOGENOM; CLU_002188_0_0_3; -.
DR Proteomes; UP000010477; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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; 1.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd00088; HPT; 1.
DR CDD; cd00130; PAS; 1.
DR CDD; cd00156; REC; 1.
DR CDD; cd17546; REC_hyHK_CKI1_RcsC-like; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.30.450.40; -; 4.
DR Gene3D; 3.40.50.2300; -; 2.
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; IPR007891; CHASE3.
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; IPR036641; HPT_dom_sf.
DR InterPro; IPR000014; PAS.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR016132; Phyto_chromo_attachment.
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; PTHR45339; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE J; 1.
DR PANTHER; PTHR45339:SF1; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE J; 1.
DR Pfam; PF05227; CHASE3; 1.
DR Pfam; PF01590; GAF; 2.
DR Pfam; PF13185; GAF_2; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF01627; Hpt; 1.
DR Pfam; PF13426; PAS_9; 1.
DR Pfam; PF00072; Response_reg; 2.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00065; GAF; 3.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00073; HPT; 1.
DR SMART; SM00091; PAS; 1.
DR SMART; SM00448; REC; 2.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF52172; CheY-like; 2.
DR SUPFAM; SSF55781; GAF domain-like; 3.
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; PS50046; PHYTOCHROME_2; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 2.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Cell inner membrane {ECO:0000256|ARBA:ARBA00022519};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:AFZ03011.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000010477};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:AFZ03011.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 188..207
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 362..383
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 400..454
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 716..852
FT /note="Phytochrome chromophore attachment site"
FT /evidence="ECO:0000259|PROSITE:PS50046"
FT DOMAIN 893..1114
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 1134..1255
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 1289..1410
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 1454..1547
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT COILED 846..883
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 1188
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 1338
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 1493
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
SQ SEQUENCE 1547 AA; 175631 MW; A5BC6E5CEA38AB3E CRC64;
MIVAPKSENE AKRIEALLEY KILDTSTEEA FDDLTKLSAY ICDAPIALIS FVDDKRQWFK
SKIGLETCEI SRDLAFCTHA ILQKDIFIIP DTKEDGRFAQ NQLVTGEPYI RFYAGIPLIN
PEGQALGTLC VIDQKPRELT LEQLEALRTI SRQVIKLLEL RRKLNFQGFF SNIKKAKNKV
QKLLFKKIAT WFIVASIILI VIGLGFYKNI SLIININNQH SITQEKIKIH LQILSNIKEA
QHGKNSYLLT GQSQFLESYN TAISQIQPQI QALNAIATNL DQKKQIAIIE NLVAIKIKQI
HQIIDLNQQN KSDLGLEIFK YYNNTENILK DIKNIIHGME QQEKKLIIKQ SADINISFRN
TVLSIIFGIC LNLITPILFY HLIYQELIKT NLIEDKLNQE NHLISTILDN ANTFVIVLDS
HSQIIRFNQA CEQALGYTFN EVRGKNFYSV FLPKKEVENL SQISEIRLNI NKLRNQEDYW
VTKDGSQLLI AWSSAILENI ENALGYQYTT ITGIDITERD RTEKHLTAQY ATTCAIAEST
TMTEAIRRIL EGICETLKWD WGEFWIVDES KNILTCLEVW HGESIVAEEF KIETLKSNFY
PEIGLPGHIW STSQPIWMTN LHQQDGFLRQ EFVQQIGLNT AFGFPIYSEN KILGVLTFFC
REIRQSETDL MMMITSIGNQ IGQFIQRKKA EEELQRQNLQ LWLLADVSDK IRQTLKLDEI
ISTSVKEVQR LLQSDRVLVL RLQADNSLIP IEEVVVPGLP IVLGQNINDP CLVETYIEKY
KQGWVSVIHD IDKSDIQQCH IEFLKQFAVK ANLVVPILLQ NQFWGLLIIH QCHSPRYWTA
WEVELLEQLA DQIGIALTQA ELLESETHQR QELEVARHQA EQASQAKSAF LANISHEIRT
PMNAILGMTG LLLETTLNRE QRDFIETIRI GGDELLTLIN EILDISKLEA GEMALETLDF
NLSTCVEDIL DLLAPLAHSK ELEIAALIDS SVPIFLQGDA SKLRQIIVNL TNNAIKFTSQ
GEVVLGLELV SQTSTDAIIL FNIKDTGIGI SLKDQSKLFK AFIQVDASTT RKYGGTGLGL
AICKQLVHLM GGEIGIESEV GKGSNFWFKI PFKKQLQPLL PQSNLEEEIL ANCSLLVVDD
NATNRKIIYH QATSWGMRVD QAENAIVALQ LLHSAAKENI LYDLVIIDMQ MPEIDGITLG
AKIKADSAIS EIPLVMLTST NGRDEVKQAL EIGFYSYLVK PVKHSRLLDN IMNILAKKLD
LESKKFTYLK NKETSLLEEN AILNTSKLRI LLAEDNVVNQ KVALKQLQNI GYKADIAANG
QEVLRLLKKI PYDLVFMDCQ MPILDGFDAT REILNWQENT FAARRRPIVI AMTANAMKED
QQRCLDAGMD DYISKPVSKD KLANVLKRWN SFIQKNYEIC SSEVIDTNNS LNQEKRSIDS
IINWEHLHQL SENNSEFELE LLQIFVNDAP AHIKSLKNAI ACDDFQSIEQ EAHHIKGSGG
NIGASQVQLT AEKLEQLAFA SQTKNMMQLV TCIEDDIAQI QEFIESL
//