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
//