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Database: UniProt
Entry: B4VMP4_9CYAN
LinkDB: B4VMP4_9CYAN
Original site: B4VMP4_9CYAN 
ID   B4VMP4_9CYAN            Unreviewed;      1210 AA.
AC   B4VMP4;
DT   23-SEP-2008, integrated into UniProtKB/TrEMBL.
DT   23-SEP-2008, sequence version 1.
DT   27-MAR-2024, entry version 86.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=MC7420_1817 {ECO:0000313|EMBL:EDX76814.1};
OS   Coleofasciculus chthonoplastes PCC 7420.
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Coleofasciculales;
OC   Coleofasciculaceae; Coleofasciculus.
OX   NCBI_TaxID=118168 {ECO:0000313|EMBL:EDX76814.1, ECO:0000313|Proteomes:UP000003835};
RN   [1] {ECO:0000313|EMBL:EDX76814.1, ECO:0000313|Proteomes:UP000003835}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PCC 7420 {ECO:0000313|EMBL:EDX76814.1,
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; DS989845; EDX76814.1; -; Genomic_DNA.
DR   RefSeq; WP_006099772.1; NZ_DS989845.1.
DR   AlphaFoldDB; B4VMP4; -.
DR   STRING; 118168.MC7420_1817; -.
DR   eggNOG; COG0784; Bacteria.
DR   eggNOG; COG3829; Bacteria.
DR   eggNOG; COG4191; Bacteria.
DR   eggNOG; COG4251; Bacteria.
DR   HOGENOM; CLU_000445_114_15_3; -.
DR   OrthoDB; 415806at2; -.
DR   Proteomes; UP000003835; Unassembled WGS sequence.
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; cd00130; PAS; 4.
DR   CDD; cd17546; REC_hyHK_CKI1_RcsC-like; 1.
DR   Gene3D; 1.10.287.130; -; 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; 5.
DR   InterPro; IPR011006; CheY-like_superfamily.
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; IPR004358; Sig_transdc_His_kin-like_C.
DR   InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR   NCBIfam; TIGR00229; sensory_box; 3.
DR   PANTHER; PTHR45339; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE J; 1.
DR   PANTHER; PTHR45339:SF1; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE J; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00512; HisKA; 1.
DR   Pfam; PF13188; PAS_8; 1.
DR   Pfam; PF13426; PAS_9; 4.
DR   Pfam; PF00072; Response_reg; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00387; HATPase_c; 1.
DR   SMART; SM00388; HisKA; 1.
DR   SMART; SM00086; PAC; 5.
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; SSF52172; CheY-like; 1.
DR   SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR   SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 5.
DR   PROSITE; PS50109; HIS_KIN; 1.
DR   PROSITE; PS50113; PAC; 4.
DR   PROSITE; PS50112; PAS; 4.
DR   PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE   4: Predicted;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW   ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000003835}.
FT   DOMAIN          54..119
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          262..314
FT                   /note="PAC"
FT                   /evidence="ECO:0000259|PROSITE:PS50113"
FT   DOMAIN          315..357
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          390..442
FT                   /note="PAC"
FT                   /evidence="ECO:0000259|PROSITE:PS50113"
FT   DOMAIN          475..528
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          550..603
FT                   /note="PAC"
FT                   /evidence="ECO:0000259|PROSITE:PS50113"
FT   DOMAIN          604..648
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          657..707
FT                   /note="PAC"
FT                   /evidence="ECO:0000259|PROSITE:PS50113"
FT   DOMAIN          725..970
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   DOMAIN          996..1112
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   COILED          6..33
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          433..478
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   MOD_RES         1045
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ   SEQUENCE   1210 AA;  135304 MW;  F9E1A41E90C1EB97 CRC64;
     MAEKTREELE QELQDLRDRL SVAEETLQAI RQGEVDALVV SGPAGDQIFT LQSADEPYRL
     FVEQMQEGAA TVTSDGMLLY CNRRLADLLQ RNLETVIGSN FKQYLNPVEV PFFQSLLQKD
     KAGYSHREFY LIASDQTEIP VELSVSPLMM EGVKVNCLIV TDLTENKRQK KIVAAEKLAR
     SIFEQVADAI VVCDQRGTII RTSMATQELC GQNPILQPFD QIFPLMFSSS TIREDNHTIS
     SPSPTSGHPF SIATILNGEI FQGIEVVFGR EDGQQFHLLL SGRALLNSKN QIQGCVVTLT
     NITARKQSEQ ALQESQERFR RAVLYSPIPI MLHAEDGEVL QINQAWTELT GYTHQDIPTI
     ADWTQKAYGT RQGLVQENID QLYHLDQPIG EGEYTIITRN GSTRIWDFSS APLGKLSDGR
     RMVISTALDV TLRKQAELEL QQANATLEVR VEERTKALQQ ELQTRHQAEQ ELRASQARFA
     GILEIASDGI ISVDANQRII LFNQGAEKMF GYRVSEVLGQ PLDLLLPNRY TIAHHQHIKT
     FSHSQGKARR MGERQAIFGR RKDGTEFPAE ASISKLTLGD QVVFTAFVQD ITERKQFEEK
     LQQSETRLKT IITATCDGIM IVDRQGQVCF ANPAAAQLFD MTPDALLNYQ WGMPLGETTE
     IELMQSSGIG RTAEMKATPI QWFSKSAYVI ALRDITKRKQ ADLSLQQAKA DAEAANQAKS
     MFLANMSHEL RTPLNIILGF TQVMSRDPAI TPEEQENLDI INKSGNHLLS LINDVLDLSK
     IEAGCISVEE SRFDLIALMR SLQEMFQHKA RAKGLQLHLN IAADVPHYIQ ADSNKLRQVL
     INLLSNAIKF TQNGSINLRV ALLKAEGNDH GSDAEDMITP PSSQTRHGTS LQASHLHFEV
     SDTGVGIAPT ELGSIFDAFI QTHAGKVANE GTGLGLAISR KFVQLMGGDI QVSSQLNQGS
     TFSFEIPVHL ADASDMEPIH THRRVIGLVP NQPCYRIIVT DDKPENRQIL VKLLTFPGLE
     VREVENGQEA LTLWQQWQPD LIWMDMRMPI MDGYQATQQI RCQSDSQTPI IIALTAYASK
     SDRASALEAG CNDYVTKPFQ VETLFAKMEE YLGVRYVYAD DHPNLSKTTQ LETSVNVNQL
     TPECLSVMPL SWIEMLSEAA QLCDDEEIFS LIEQIPPEET LLITTLSHLA HNFQFDPIIQ
     LAQSVINSDK
//
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