ID B4W013_9CYAN Unreviewed; 974 AA.
AC B4W013;
DT 23-SEP-2008, integrated into UniProtKB/TrEMBL.
DT 23-SEP-2008, sequence version 1.
DT 27-MAR-2024, entry version 72.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=MC7420_3506 {ECO:0000313|EMBL:EDX72434.1};
OS Coleofasciculus chthonoplastes PCC 7420.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Coleofasciculales;
OC Coleofasciculaceae; Coleofasciculus.
OX NCBI_TaxID=118168 {ECO:0000313|EMBL:EDX72434.1, ECO:0000313|Proteomes:UP000003835};
RN [1] {ECO:0000313|EMBL:EDX72434.1, ECO:0000313|Proteomes:UP000003835}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 7420 {ECO:0000313|EMBL:EDX72434.1,
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; DS989864; EDX72434.1; -; Genomic_DNA.
DR RefSeq; WP_006104393.1; NZ_DS989864.1.
DR AlphaFoldDB; B4W013; -.
DR STRING; 118168.MC7420_3506; -.
DR eggNOG; COG0745; Bacteria.
DR eggNOG; COG2114; Bacteria.
DR eggNOG; COG4753; Bacteria.
DR eggNOG; COG5002; Bacteria.
DR HOGENOM; CLU_000445_114_26_3; -.
DR OrthoDB; 9809348at2; -.
DR Proteomes; UP000003835; Unassembled WGS sequence.
DR GO; GO:0004016; F:adenylate cyclase activity; IEA:UniProt.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR GO; GO:0009190; P:cyclic nucleotide biosynthetic process; IEA:InterPro.
DR CDD; cd07302; CHD; 1.
DR CDD; cd16922; HATPase_EvgS-ArcB-TorS-like; 1.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd00130; PAS; 1.
DR CDD; cd17574; REC_OmpR; 1.
DR CDD; cd17536; REC_YesN-like; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.40.50.2300; -; 2.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 3.30.70.1230; Nucleotide cyclase; 1.
DR Gene3D; 3.30.450.20; PAS domain; 1.
DR InterPro; IPR001054; A/G_cyclase.
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; IPR029787; Nucleotide_cyclase.
DR InterPro; IPR000014; PAS.
DR InterPro; IPR000700; PAS-assoc_C.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR013656; PAS_4.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR NCBIfam; TIGR00229; sensory_box; 1.
DR PANTHER; PTHR43047:SF72; OSMOSENSING HISTIDINE PROTEIN KINASE SLN1; 1.
DR PANTHER; PTHR43047; TWO-COMPONENT HISTIDINE PROTEIN KINASE; 1.
DR Pfam; PF00211; Guanylate_cyc; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF08448; PAS_4; 1.
DR Pfam; PF00072; Response_reg; 2.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00044; CYCc; 1.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 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; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR SUPFAM; SSF55073; Nucleotide cyclase; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 1.
DR PROSITE; PS50125; GUANYLATE_CYCLASE_2; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50113; PAC; 1.
DR PROSITE; PS50112; PAS; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 2.
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 4..123
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 167..203
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 246..298
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 323..541
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 579..696
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 736..862
FT /note="Guanylate cyclase"
FT /evidence="ECO:0000259|PROSITE:PS50125"
FT COILED 143..177
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 289..323
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 58
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 629
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 974 AA; 109700 MW; 789B0EB09610E385 CRC64;
MPAKILVVDD EPDLELLIRQ KFRKKIRRQE LQFIFAHNGV DALETLHAQP DIDMVLTDIN
MPEMDGLTLL THLAQDYPTT KAVILSAYGD MENIRKAMNL GAFDFLTKPI DFQDLDITTH
KTLNHVQQLK AAQQQEYLAQ QAQADLLENL RQEVIERQRI QEELRASERQ LAQFLEAVPV
GLFVVDAEGQ SYYANQRAQQ LVGKGMIPGA TVEELSQVYQ IYVAGTHQLY PTEKNPIVQA
LRGERVTVDN MEIHHGEQVI PLEVWATPIY NEQGEIVYAI AAFQDISLHK QAEAERLQFT
QALEQQNAAL QRLDQLKDEF LANTSHELRT PLNGIIGITE SLIDGAAGSL SPVQIANLAM
VVSSGKRLNS LINDILDFAK LKNHDIELHR KSVDFRQITE VVLTLSRPLI QGKSLELNNE
IPADFPGIDG DENRLQQIMY NLVGNAIKFT ESGSITVSAT QQQNMAEVTV ADTGIGISPD
KFEDIFKSFE QLNASVSYPS RGTGLGLSIT KQLIELHGGR IRVESEVGQG SRFIFTLPLS
FQPIASSSEY RTDITKVRDY SNSFPSELLP LMSKTGEFTI LVVDDEPINL QVVTNHLSVH
NYAIVQATSG IEALAKIEQG FKPDLVILDI MMPKMSGYEV CQKIRQCFPA TEMPIILLTA
KEQVSDLVEG LSLGANDYLT KPISKHELIA RIKTHLHLSN INRAYGRFVP QEFLRFLGYE
SIVDVRLGDQ VQQDMSIMFA DIRNFTTLSE SMSPQDNFNF LNSYLKQVGP IIRKHQGFID
KYIGDAIMAL FPQTADDGLK AAIEIQKQVT RYNRDREKAG YPSITIGIGL HTGSLMLGTI
GEQQRMETTV ISDTVNLASR LEDLTKIYGA SILISGYTLF CLEDQSQYHY RFIGQVQVKG
KKHLVPVFEI FDAEPEYIIQ FKENTKTTFE AGIVNFNQNK IDVALRIFEH IVEINWRDRA
ALNYIKLCER TRPQ
//
