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Database: UniProt
Entry: B4VSP9_9CYAN
LinkDB: B4VSP9_9CYAN
Original site: B4VSP9_9CYAN 
ID   B4VSP9_9CYAN            Unreviewed;      1055 AA.
AC   B4VSP9;
DT   23-SEP-2008, integrated into UniProtKB/TrEMBL.
DT   23-SEP-2008, sequence version 1.
DT   27-MAR-2024, entry version 87.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=MC7420_2099 {ECO:0000313|EMBL:EDX75095.1};
OS   Coleofasciculus chthonoplastes PCC 7420.
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Coleofasciculales;
OC   Coleofasciculaceae; Coleofasciculus.
OX   NCBI_TaxID=118168 {ECO:0000313|EMBL:EDX75095.1, ECO:0000313|Proteomes:UP000003835};
RN   [1] {ECO:0000313|EMBL:EDX75095.1, ECO:0000313|Proteomes:UP000003835}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PCC 7420 {ECO:0000313|EMBL:EDX75095.1,
RC   ECO:0000313|Proteomes:UP000003835};
RA   Tandeau de Marsac N., Ferriera S., Johnson J., Kravitz S., Beeson K.,
RA   Sutton G., Rogers Y.-H., Friedman R., Frazier M., Venter J.C.;
RL   Submitted (JUL-2008) 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; DS989850; EDX75095.1; -; Genomic_DNA.
DR   AlphaFoldDB; B4VSP9; -.
DR   STRING; 118168.MC7420_2099; -.
DR   eggNOG; COG0745; Bacteria.
DR   eggNOG; COG2205; Bacteria.
DR   eggNOG; COG5002; Bacteria.
DR   HOGENOM; CLU_000445_114_15_3; -.
DR   Proteomes; UP000003835; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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; cd16922; HATPase_EvgS-ArcB-TorS-like; 1.
DR   CDD; cd00082; HisKA; 1.
DR   CDD; cd00130; PAS; 2.
DR   CDD; cd17546; REC_hyHK_CKI1_RcsC-like; 1.
DR   Gene3D; 1.10.287.130; -; 1.
DR   Gene3D; 3.30.450.40; -; 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; 4.
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; 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; 3.
DR   PANTHER; PTHR43047:SF72; OSMOSENSING HISTIDINE PROTEIN KINASE SLN1; 1.
DR   PANTHER; PTHR43047; TWO-COMPONENT HISTIDINE PROTEIN KINASE; 1.
DR   Pfam; PF01590; GAF; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00512; HisKA; 1.
DR   Pfam; PF00989; PAS; 2.
DR   Pfam; PF08447; PAS_3; 1.
DR   Pfam; PF00072; Response_reg; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00065; GAF; 1.
DR   SMART; SM00387; HATPase_c; 1.
DR   SMART; SM00388; HisKA; 1.
DR   SMART; SM00086; PAC; 3.
DR   SMART; SM00091; PAS; 3.
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; SSF55781; GAF domain-like; 1.
DR   SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR   SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 3.
DR   PROSITE; PS50109; HIS_KIN; 1.
DR   PROSITE; PS50113; PAC; 3.
DR   PROSITE; PS50112; PAS; 3.
DR   PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
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:UP000003835};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          221..291
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          294..346
FT                   /note="PAC"
FT                   /evidence="ECO:0000259|PROSITE:PS50113"
FT   DOMAIN          347..391
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          402..452
FT                   /note="PAC"
FT                   /evidence="ECO:0000259|PROSITE:PS50113"
FT   DOMAIN          453..523
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          527..579
FT                   /note="PAC"
FT                   /evidence="ECO:0000259|PROSITE:PS50113"
FT   DOMAIN          597..825
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   DOMAIN          851..967
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   MOD_RES         900
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ   SEQUENCE   1055 AA;  117911 MW;  98FA3D82556D58A2 CRC64;
     MAMVIELCQA ISGEIRLQPL LSTLIQIAFE TTEAQSVTLI LPQPEGLVVA ARGVRGTNPS
     ILPLTPIESS PEIPLMLVEY VWHHPDILIV SDDTTDIKRW SMIALNLGDE GNESGFSTIR
     AGNKDNSETR PYNLNTQNST RSPLSVLCAP LTVGNQGIGI LYLENNQTRG VFTRDRVAIV
     QLLCVQAASA LKNAQAYNHL ENHSRILENT VEQQKQQLQH SEFRYRAIIE DQSELICRYS
     ADGILTFVNE VYCRYFGKTP KELIGHRFVP LIHPDDQAVL EGFIAELNPN NPVGIVEHRV
     ILESGEIRWQ QWSDRAIFDN QGRLLEFQAV GRDITDCKLT EARLRQSEAR LNAIVSSTSD
     GIMIVDRQGQ VLFTNPAAAN LLNQDVENLL NYNFGLPVGV NQTTELGIVR ADGQLSFAEM
     SVVETEWEGE SVFEICLRDV TERQRAEAAL RESEERFRAI FEQAAVGIAL GTPSGQLIRV
     NQRFCDLVGY EESELLQLSF PDITHPDDRA AELNDLTQLL AGQRSTYSRE KRFIRKDGQW
     QWVNVAVSLV RTWMDTPNYI IGVVEDIQQR KQTEVALQQA LDAAEAANHG KSEFLANMSH
     ELRTPLNAIL GFTQLMARDA SLNQDQQDYL GIITRSGEHL LDLINNVLNM SKIEAGRISL
     SENSFDLYSL VDSIAEMLRL KALSKGVQLM VERTANVPNY GMADEGKLRQ ILINLVGNAV
     KFTSQGRVIL RVQEISDRIT APTNTDTQSR LFFEVEDTGV GIPPDELDTL FQAFVQTKTS
     QRSQSGTGLG LAISRRFVQL MGGDITINST PGQGTLVKFD IPIGIVLQDQ TPRQPLSQQV
     IGIAPDQPNY RILVVEDQWA NRKPLVKFLE SLGLDVREAD NGQVAVAIWE HWHPHLIWLD
     MRMPVMNGYE ATQLIKSHPL GKTTVIIALT ASAFDEERTA ILDAGCDDFV AKPFRTDAIL
     EKMGQHLGLR YRYENAAPPS SDAETPILTP EDLKVMPTNW IAQLHQAAIQ LNNKQIIQLI
     EQIPPEQMLF AKALTDLVNN FRCDVIMDIA HKAIS
//
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