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Database: UniProt
Entry: A0A0V7ZM53_9CYAN
LinkDB: A0A0V7ZM53_9CYAN
Original site: A0A0V7ZM53_9CYAN 
ID   A0A0V7ZM53_9CYAN        Unreviewed;      1057 AA.
AC   A0A0V7ZM53;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   27-MAR-2024, entry version 34.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=BC008_23980 {ECO:0000313|EMBL:KST66042.1}, BC008_42375
GN   {ECO:0000313|EMBL:KST65569.1};
OS   Mastigocoleus testarum BC008.
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Hapalosiphonaceae;
OC   Mastigocoleus.
OX   NCBI_TaxID=371196 {ECO:0000313|EMBL:KST65569.1, ECO:0000313|Proteomes:UP000053372};
RN   [1] {ECO:0000313|EMBL:KST65569.1, ECO:0000313|Proteomes:UP000053372}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BC008 {ECO:0000313|EMBL:KST65569.1,
RC   ECO:0000313|Proteomes:UP000053372};
RA   Guida B.S., Garcia-Pichel F.;
RT   "Draft Genome of the Euendolithic (true boring) Cyanobacterium
RT   Mastigocoleus testarum strain BC008.";
RL   Genome Announc. 0:0-0(2015).
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   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KST65569.1}.
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DR   EMBL; LMTZ01000107; KST65569.1; -; Genomic_DNA.
DR   EMBL; LMTZ01000100; KST66042.1; -; Genomic_DNA.
DR   RefSeq; WP_058183882.1; NZ_LMTZ01000107.1.
DR   AlphaFoldDB; A0A0V7ZM53; -.
DR   Proteomes; UP000053372; 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; cd00082; HisKA; 1.
DR   CDD; cd00130; PAS; 3.
DR   CDD; cd00156; REC; 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; 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; IPR004358; Sig_transdc_His_kin-like_C.
DR   InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR   NCBIfam; TIGR00229; sensory_box; 3.
DR   PANTHER; PTHR43065:SF10; PEROXIDE STRESS-ACTIVATED HISTIDINE KINASE MAK3; 1.
DR   PANTHER; PTHR43065; SENSOR HISTIDINE KINASE; 1.
DR   Pfam; PF01590; GAF; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00512; HisKA; 1.
DR   Pfam; PF00989; PAS; 1.
DR   Pfam; PF08448; PAS_4; 1.
DR   Pfam; PF13188; PAS_8; 1.
DR   Pfam; PF13426; PAS_9; 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; SM00091; PAS; 4.
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); 4.
DR   PROSITE; PS50109; HIS_KIN; 1.
DR   PROSITE; PS50113; PAC; 1.
DR   PROSITE; PS50112; PAS; 2.
DR   PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:KST65569.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW   ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000053372};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          318..388
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          560..629
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          631..683
FT                   /note="PAC"
FT                   /evidence="ECO:0000259|PROSITE:PS50113"
FT   DOMAIN          696..918
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   DOMAIN          938..1054
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   MOD_RES         989
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ   SEQUENCE   1057 AA;  120425 MW;  B79319434762A339 CRC64;
     MNSLLSKKEL ARIEALYQYR ILDTSPEEEF DDLAFLAAQI CQTPIALINL IDINRQWFKA
     KVGLDVEEMP RSMGFCPLCI EQNDVLIIPD TLADERFANS PVVQSYPFAR FYAGVPLITY
     QGHDIGTLCV VDTEPREISE QQIKSLQAIS RQIIKQLEIK RNLSELVDIK KEYQQAQVAL
     RDSQGIINSF FESAPMMMGI IEIVDDDILH ISGNAAAAEL FEMTPEEMGN RLLSEMNLPQ
     QYLQAWVQRY LESCSENLPF TFEDSYDKPT GKIWLKITVS PIPCDNNRQR FAYFVEDITE
     RKRVESERLQ LLVNEQAARN RITNIFESIT DGFVALDRQW CFTYVNQQAE LLLQRTRKQL
     LGKSIWEEFP ESLRSKFNKE YNHALSAQVS VEFEEFYAPL NIWFSVHAYP SKEGLSIYFQ
     DITERKNYEE NLRWKEALLR SMNSVSPLAF YVVDHTTENI LFANERFREL WGIEQLKEAM
     ESSTLKHADV MKACQKSMGI IPFDTCLPES MEKCICEDEI FLPDGRTIRR FSRQILNDGL
     DFGRLYILED ITARKQVEQQ IREQAALLDL TTDAIVLRDL SNHILLWNKS AEKLYGWKEE
     EVIGKNANQL LKTEFKHSEK ILSSVLKKGI WQGELKKISK FGKEIIVDSC WTLVKDENRK
     AKSIMVVDTD ITQKKQLETQ FLRAQRMESI GTLASGIAHD LNNVLSPILM SAQLLKLKSQ
     DESIIEMLSI VEKNAKRGAN LVKQVLSYAR GIEGDRTLLQ MKHLILEMQQ IIDQTFPKSI
     RTEIDIQPDL WDVYGDNTQV HQVLMNLCLN ARDAISEYGT LRISVENIFI DENYAQMNLE
     AKVGSYVLLK VEDTGIGIPN DLLGRIFEPF FTTKEFGQGT GLGLSTVMGI IKGHGGFISV
     SSRVGQETSF HVYLPASNVS LEQLVEDIAA TPSGCGELIL VVDDEPAIRE ITKNSLEHHN
     YQVMTASDGI EAVAIYAQYR SKISAAIIDM MMPNMDGATT ISTLRKMNPT VRIVAVSGLM
     NSENLPGKNT DNAVTFLQKP YTTQALLQKL HKVLPEN
//
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