ID B4VIS0_9CYAN Unreviewed; 1855 AA.
AC B4VIS0;
DT 23-SEP-2008, integrated into UniProtKB/TrEMBL.
DT 23-SEP-2008, sequence version 1.
DT 27-MAR-2024, entry version 89.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=MC7420_7957 {ECO:0000313|EMBL:EDX78219.1};
OS Coleofasciculus chthonoplastes PCC 7420.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Coleofasciculales;
OC Coleofasciculaceae; Coleofasciculus.
OX NCBI_TaxID=118168 {ECO:0000313|EMBL:EDX78219.1, ECO:0000313|Proteomes:UP000003835};
RN [1] {ECO:0000313|EMBL:EDX78219.1, ECO:0000313|Proteomes:UP000003835}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 7420 {ECO:0000313|EMBL:EDX78219.1,
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};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the phytochrome
CC family. {ECO:0000256|ARBA:ARBA00006402}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; DS989842; EDX78219.1; -; Genomic_DNA.
DR RefSeq; WP_006098654.1; NZ_DS989842.1.
DR STRING; 118168.MC7420_7957; -.
DR eggNOG; COG2203; Bacteria.
DR eggNOG; COG2205; Bacteria.
DR eggNOG; COG2905; Bacteria.
DR eggNOG; COG5002; Bacteria.
DR HOGENOM; CLU_001445_1_0_3; -.
DR OrthoDB; 415806at2; -.
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; cd04620; CBS_two-component_sensor_histidine_kinase_repeat1; 1.
DR CDD; cd17774; CBS_two-component_sensor_histidine_kinase_repeat2; 1.
DR CDD; cd16922; HATPase_EvgS-ArcB-TorS-like; 1.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd00130; PAS; 5.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.30.450.40; -; 2.
DR Gene3D; 3.40.50.2300; -; 1.
DR Gene3D; 3.10.580.10; CBS-domain; 3.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 3.30.450.20; PAS domain; 6.
DR InterPro; IPR000644; CBS_dom.
DR InterPro; IPR046342; CBS_dom_sf.
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; IPR013767; PAS_fold.
DR InterPro; IPR013655; PAS_fold_3.
DR InterPro; IPR016132; Phyto_chromo_attachment.
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; PTHR43047:SF79; HISTIDINE KINASE; 1.
DR PANTHER; PTHR43047; TWO-COMPONENT HISTIDINE PROTEIN KINASE; 1.
DR Pfam; PF00571; CBS; 4.
DR Pfam; PF01590; GAF; 2.
DR Pfam; PF02518; HATPase_c; 2.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF00989; PAS; 1.
DR Pfam; PF08447; PAS_3; 2.
DR Pfam; PF08448; PAS_4; 1.
DR Pfam; PF13426; PAS_9; 1.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00116; CBS; 3.
DR SMART; SM00065; GAF; 2.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00086; PAC; 4.
DR SMART; SM00091; PAS; 5.
DR SMART; SM00448; REC; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF54631; CBS-domain pair; 2.
DR SUPFAM; SSF52172; CheY-like; 1.
DR SUPFAM; SSF55781; GAF domain-like; 2.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 5.
DR PROSITE; PS51371; CBS; 3.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50113; PAC; 4.
DR PROSITE; PS50112; PAS; 5.
DR PROSITE; PS50046; PHYTOCHROME_2; 2.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW CBS domain {ECO:0000256|PROSITE-ProRule:PRU00703};
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 23..101
FT /note="CBS"
FT /evidence="ECO:0000259|PROSITE:PS51371"
FT DOMAIN 110..170
FT /note="CBS"
FT /evidence="ECO:0000259|PROSITE:PS51371"
FT DOMAIN 300..361
FT /note="CBS"
FT /evidence="ECO:0000259|PROSITE:PS51371"
FT DOMAIN 417..552
FT /note="Phytochrome chromophore attachment site"
FT /evidence="ECO:0000259|PROSITE:PS50046"
FT DOMAIN 583..657
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 659..711
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 712..765
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 767..818
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 819..860
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 895..945
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 985..1030
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 1102..1179
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 1181..1234
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 1254..1390
FT /note="Phytochrome chromophore attachment site"
FT /evidence="ECO:0000259|PROSITE:PS50046"
FT DOMAIN 1431..1703
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 1737..1853
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT MOD_RES 1786
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1855 AA; 211086 MW; 7A1C2FA9331C78C9 CRC64;
MASSPHLPNQ PWCFHSPQLD DILDRTPVTV TLDTPVVEVL ARMSQVQGCS CSQEGEKTPE
SPQNPLLSPS TSCVLVTQGT QLVGIFTERD VVRLTAQGRN LAGVSIRQVM SPPDYRLKSS
EFRDVFSVLG ILKQYQIRHL PVVDDQEQLL GLITLSTLRS VIEPSHLLKL RTVDEVMNRT
VIQATVDTSV LKLAQLMARH RVSCVVICQA DCSRHLEKST LVLTPQPPSF PPARGENSQP
LSLQERGLER GFSDPVKSNI CQEFPAGNQQ KPVGIITERD IVQFQVLGVN LSGLQAKDVM
SQPLFYLRTQ DNLWHAHQEM QRRYVRRLVV TGDQGELLGI VTQTRLLQVL DPMEMYGVID
QLQQVIGQLE AEKIELLESR NTQLEELVQS RTHQLQKQAE REHILRSIAQ RIRCFLKLPD
IFQATVKEVR QLLHCDRVLV YQFAEDWSGE IVAESVGDFP SVLGSQVRDA YFQETKGADY
LNGRRQVAHN IYHQGLTPCH LELLEQFQVK AILTVPIIIN EQLWGLLVAH HCAAPRPWEP
QELDLLEQLS VQIAIAIQQA NAFSQLQTEL AERQKAEQLA KATQERLHYL LSASPTAIYS
RQFIPPYQTT FISDNITALI GYTPGEILEQ PDFWLNHIHP QDLPTVLTGF AQLFQQGYSI
QEYRFKQKNG EYLWLQDDWK LIRNDQGIPQ EIIGAWLDIS HRVQAQEHAQ TSEKLLELFY
ESAPVGLCIT DEQWRLVRVN PAFCQLFAYP RDYLLGRSLT EFLDPHHSGE WQVRRHDGKF
IDIQVTTGPI MQQGERCLRV TTVTDITERK KAEQAIQSMA GQLSTVIDTV GEGITLSNSQ
GKFRIFNHQM QQITGYTRQE ANRCENFMAK LYPDPLLYQQ VKQWQKSPSK KRKLRTFETT
FCDKNGVQKT LLVSHSIIHQ DNQLLFLSAY RDISDRKQAE ESLKHLNEAL EKRVQERTTA
LEQTVEHLHR EIKERQQTEL ALQDSHRKIN NILESITEGF FALDQDWRFT HFNSLLAPLI
NRPVSDMIGR CIWDEFPDAM GTKFETIYRQ AAREQKPMAF EELYASNNTW YEVRVYPSED
GLSVYFRDIS DRKKAELALQ ESQRFIQRIA DTNPNVLYIY DIAEQRNIYI NRSVAQVLGY
SPEQIQQMES KLFESLMHPD DLAQVLRQHQ RFDTAKDGDI IECEYRMRHA NGQWRWLYSW
DTIFTRTSEG KPKQILGTAS DITSRKQVEE TLRQQVERER LISAMSRRIR QSLDLETILT
TTVEEIQQLL MADRVLVYQL FEDNRGRVIA EGVASGFPQL LNSIFPAEAF PPTCYQNYVQ
GKVYTLADRD REDVLPCMVD FMREYAIRAK LVVPIVQQDI LWGLLIVHQC SHPREWQTWE
IELLVSLATQ LAIAIKQSQL YEQLRHNNDI LATTNAELAH ATRLKDEFLA NMSHELRTPL
NAILGLSESL QEEVYGEITE KQRKSLATIE KSGRHLLELI NDILDLAKIE SGKLELNLTA
VRISQLCDAS LSLIKPLALE KNITLSGNIA AGLGTILGDE RRLQQVLINL LSNAVKFTPE
GGQVTVEIRK QDGGDERDKE VNATFSQGGF CSNVTISSQK KIPKPAPTNH TLEGEEELTF
NTSPNEMLYI SVSDTGIGIA KEHREKLFQS FVQIDSSLSR RHQGTGLGLA LVRRIVELHG
GWVTVESEIG KGSCFTVRLP WRSHPVNHSI SYPAEKATLG CSVSDIEDTT LSRTTPLILL
AEDNEANTQT LSDYLQGIGY EMIMAKDGKE AVQLSQRRKP DLILMDIQMP ELDGLSATQQ
IRANPRTATI PIIAITALAM SGDREKCLAA GVSYYMTKPV NLKKLATIIN ALLTG
//
