UniProt: K9V5A3

Database: UniProt
Entry: K9V5A3_9CYAN

LinkDB:  K9V5A3_9CYAN 
Original site:  K9V5A3_9CYAN

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Ontology (3)   
   GO (3)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
Gene (1)   
   KEGG GENES (1)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (35)   
   InterPro (16)   
   Pfam (8)   
   PROSITE (5)   
   SMART (6)   
All databases (41)   

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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
//

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