ID A0A0V7ZPY0_9CYAN Unreviewed; 2653 AA.
AC A0A0V7ZPY0;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=BC008_25165 {ECO:0000313|EMBL:KST66262.1};
OS Mastigocoleus testarum BC008.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Hapalosiphonaceae;
OC Mastigocoleus.
OX NCBI_TaxID=371196 {ECO:0000313|EMBL:KST66262.1, ECO:0000313|Proteomes:UP000053372};
RN [1] {ECO:0000313|EMBL:KST66262.1, ECO:0000313|Proteomes:UP000053372}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BC008 {ECO:0000313|EMBL:KST66262.1,
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 -!- SIMILARITY: In the N-terminal section; belongs to the phytochrome
CC family. {ECO:0000256|ARBA:ARBA00006402}.
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:KST66262.1}.
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DR EMBL; LMTZ01000098; KST66262.1; -; Genomic_DNA.
DR RefSeq; WP_058183831.1; NZ_LMTZ01000098.1.
DR OrthoDB; 446897at2; -.
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; cd16922; HATPase_EvgS-ArcB-TorS-like; 1.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd00130; PAS; 7.
DR CDD; cd17546; REC_hyHK_CKI1_RcsC-like; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.30.450.40; -; 5.
DR Gene3D; 3.40.50.2300; -; 2.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 3.30.450.20; PAS domain; 8.
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; 8.
DR PANTHER; PTHR43047:SF72; OSMOSENSING HISTIDINE PROTEIN KINASE SLN1; 1.
DR PANTHER; PTHR43047; TWO-COMPONENT HISTIDINE PROTEIN KINASE; 1.
DR Pfam; PF01590; GAF; 4.
DR Pfam; PF13185; GAF_2; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF00989; PAS; 1.
DR Pfam; PF08447; PAS_3; 3.
DR Pfam; PF08448; PAS_4; 2.
DR Pfam; PF13426; PAS_9; 2.
DR Pfam; PF00072; Response_reg; 2.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00065; GAF; 5.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00086; PAC; 7.
DR SMART; SM00091; PAS; 8.
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; SSF55781; GAF domain-like; 5.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 8.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50113; PAC; 6.
DR PROSITE; PS50112; PAS; 8.
DR PROSITE; PS50046; PHYTOCHROME_2; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 2.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Coiled coil {ECO:0000256|SAM:Coils};
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:UP000053372};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 7..123
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 156..228
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 661..731
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 735..787
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 969..1016
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 1043..1093
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 1264..1337
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 1341..1394
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 1395..1464
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 1523..1580
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 1597..1649
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 1657..1731
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 1733..1785
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 1786..1856
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 1859..1911
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 1931..2097
FT /note="Phytochrome chromophore attachment site"
FT /evidence="ECO:0000259|PROSITE:PS50046"
FT DOMAIN 2138..2400
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 2426..2554
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT COILED 634..664
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 56
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 2475
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 2653 AA; 300851 MW; F0285AC1209A16A0 CRC64;
MDEENIKILL VDDRAENLHF LSEIFAGKGY SLVRAISGKL ALNAAFTSPP NLILLDIVMP
GLDGYQVCKY LKSYEKTRDI PIIFTSVKNE VFDKVKALRL GAADYLTKPL QAEEILVRVE
NQLTIQKLQK QIKAQNLQLQ TEIRERRKVT LQLDHRNQQI ESILNNAQVG ICLTDESGSL
VDVNPTYCQL YGFSKDELIG NKFKLNYIGS DPLEVIEKIP YRYELGNNNY GRGKRKNEYT
IKQKNGNQLT VEMARGNFDS YDGKSFAVTT LIDVTEKKLA EAARVSREAY LAGLVDVQRA
LLSFDGSREL ETQIIQILGN VANASRAYIF EIQRQDNGIK SVREKAEWSK DEFKSNNHSS
LVQSRLREKL FTTWIKLLAR GEIICGKVSG LSKLAQEILG GNSVLSTLVL PMIIKGELFG
FIGFDNCQEA KVWDNYEISF LQAAATAISL ARQRQQAEEK LQQQLERSLF IRKITDKIRS
NIDTKTIVEI STKEIGQALN VSRALISSYT DIPQPQLLRL GEFTAPSCSS HKKVHVSQIL
TANNHHIHKV LSQDRAIASQ DVYKEPLLEN VRDICRILEM KSMLAVRTSY QGKPNGIIGL
HQCDRYREWK VEEIELLESI ASQLGIALAQ AQILEQEQIA RSELDRQNLQ LQEEIRERLE
SEERFRSLVE TSSGWVWEVD RDFIYTYASP RVFDLLGYHP HEVLGKTPFD LVSPEEANRL
KGVFNSKIAA RHPFQALEKT NLHKNGHQVI LETNSVPVFD AWGKFSGYRG VDRDITERKH
ANEAIRTTAI KLRNHNIVLT QLAKNQVIYQ GDLKLALREI TEAAARNVNV ERASIWLYND
SCSVVRCLDL FESSCSRHSE GSELVVADYP NYFQALEADQ PIVTSQPILD HRTQQLTESY
LTPLDITATL SIPLRLGGIT TGILSLEQVG NEHHWTQEDE NFARSLGNLV YLALEARSRQ
NAEAARRASE VMLASAFRAS PDPIFLSALP QNSYIEVNDS FCNFFGYTRQ EVIDRTPEEV
NIWVNLKEYH QISQLLGQIE TIRNHEVEIR KKNGEICTAL LSADSIEIGD QQHVLATVRD
ITERKQAENE NRLLLLTTQA ISRAADVDHA LAQILRLICN NISWDFAEAW NPNNDGTFLE
YCLGWYGYQN NLEEFCLYSE SITLTSGIGI AGKVWQSKQP QWLEDVSQTF PPNFVRATVA
DRVGLKAGFG VPILANEQVL AVLVFFKSDR APVDIRLLEL VGAVAAQLGT LIQRKQAEAA
HRESEERLQL ALEASDLGLW DWNLVNDKIY RDWRWWKMLG YDKETITNNN NASSEELMHP
EDIPKIKQAL TDYLAGNSPV YEVEFRMRSR FNEWKWIQSQ GKVVERNHWG EALRMTGTHK
DITERKTLER EIALREARLN AFFSCAPVGL TILDKELRFL QINELLAEIN GISVEEHLGR
TINEVLPQIA PVIAPVYKQV MTDGQPVLNL ELSGTSLEEP NTLRHFLVSY FPIPSENERC
VDVGTVLFEI TDRKRAEAAL QEREEEFRAI FENAAVGIAQ VAPDGFFIKV NQQFCQIVGY
SKAELLQRTC QDITHPASLE KYLDYACLAG KGDIDVFSME KCFIRKNGEP IWTNLTASVV
REPSGKLKYC IGVVEDISER KAVLRERKRV EQELRLASER LQYLLTSSPA VIFSTKPSED
FANTFISENV KAMVGYEARE FLEHSNFWFS HIHPDDIERV HCELSKLCEQ KYSSFEYRFL
HKSGTYHWFY EQVRLIHDDL GNPIECVGYW VDISERKQAE LNLQASQRRY QTLAEASPVC
IFHDDADGNC FYINQRWTEI TGLPQSAALG KGWLEVIHPD DRERVFITWQ KAVDNKTKYQ
CEHRVLGANG KVIWVIYQAL AEYNENGEVN SYIGTITDIT ERKEAEVALR ESAEREKAIS
QVIQNMRQTL DLESIFTTTT QELRQVLNCD RVVVYRFNPD WSGEFVAESV GSPWVSAMMK
NKGKDSSGLA GDTLDNEGCV VQMLDSDDEQ LVDTYLQETQ GGAYSRGVSF LCVPDIYKAS
FESCYINFLE RFQARAYITV PIFCGNKIWG LLASYQNSGP RHWKTGEINI VVQIGNHLGV
ALQQGQLLAQ TRNQSEALQQ AVIAADAANR AKSEFLANMS HELRTPLNAI LGFTQIMSRD
RSILNEHQQN VEIINRAGEH LLNLINDILE MSKIEAGRTT LNVTSFDLVA LLDNLQDMLQ
VRATSKGLQL VFEYDVRQLT RYIQTDSSKL RQVLLNLLGN AIKFTKTGNV TLKVKFNIDE
PELPKKLENN TAARNQSEQQ MDRIGTAAVD PSQSTNNESD IPSQFLIFDV IDTGAGISSE
EMDLLFEAFG QTETGRKSQQ GTGLGLAISR KYIKLMGGDI SVTSIIGMGS TFSFYIPVEL
SCSQEIISTT NYRQVIGLAV NQPQYRILVV DDATESRLLL VKSLSSLGFS VKEAVNGKEA
IASWESWRPH LILMDIRMPV LDGYEATRII KNKQSQIKAL NTEHSASSFQ TVIVALSANV
FEEDRKAMIN AGCDDFVNKP FREEVLLEKL RYHLGLKYIY QENSHQKSAE NQTTPEEVSK
LLAQMPQEWL QELNYAAAQG SDCTISGLLE QIPQTKALLA EFLIDLNHNF QFERIMELIK
SININSDQYS YTP
//
