ID A0A1Q8Z9F0_9CYAN Unreviewed; 2153 AA.
AC A0A1Q8Z9F0;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 24-JAN-2024, entry version 27.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=BST81_18070 {ECO:0000313|EMBL:OLP16902.1};
OS Leptolyngbya sp. 'hensonii'.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Leptolyngbyales; Leptolyngbyaceae;
OC Leptolyngbya.
OX NCBI_TaxID=1922337 {ECO:0000313|EMBL:OLP16902.1, ECO:0000313|Proteomes:UP000186296};
RN [1] {ECO:0000313|EMBL:OLP16902.1, ECO:0000313|Proteomes:UP000186296}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=hensonii {ECO:0000313|Proteomes:UP000186296};
RA Hamilton T.L., Klatt J.M., De Beer D., Macalady J.;
RT "Physiology of photosynthesis in the novel isolate Oscillatoriales
RT cyanobacterium hensonii.";
RL Submitted (NOV-2016) 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 -!- 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:OLP16902.1}.
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DR EMBL; MQTZ01000045; OLP16902.1; -; Genomic_DNA.
DR RefSeq; WP_075599913.1; NZ_MQTZ01000045.1.
DR STRING; 1922337.BST81_18070; -.
DR Proteomes; UP000186296; 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 CDD; cd16922; HATPase_EvgS-ArcB-TorS-like; 1.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd00130; PAS; 1.
DR CDD; cd17546; REC_hyHK_CKI1_RcsC-like; 1.
DR CDD; cd14014; STKc_PknB_like; 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; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 3.30.450.20; PAS domain; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR041664; AAA_16.
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; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR000014; PAS.
DR InterPro; IPR000700; PAS-assoc_C.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR013655; PAS_fold_3.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR PANTHER; PTHR43642; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE G; 1.
DR PANTHER; PTHR43642:SF1; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE G; 1.
DR Pfam; PF13191; AAA_16; 1.
DR Pfam; PF01590; GAF; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF08447; PAS_3; 1.
DR Pfam; PF00069; Pkinase; 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; 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; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50113; PAC; 1.
DR PROSITE; PS50112; PAS; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
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:UP000186296};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 7..275
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 1519..1595
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 1598..1649
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 1692..1912
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 1938..2058
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT COILED 1640..1692
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 1987
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 2153 AA; 242860 MW; EA375B7D95B95F2C CRC64;
MMEIAGYRCI EQLHDSAKTL IYRACRHRAR QLPGEAGAPT VVIKLLRTLY PSLTELLRFR
NQYAITKYLA RPGIVRSYSL EPYQNGYALV MEDFGGISLR EYLRIEPLSL DQFFNIALQL
ADILQELYLQ RVIHKDINPA HILINPTTQR VQLIGFSLAS LLPREIQDGH NPQVLEGTLA
YLSPEQTGRM NRGMDYRTDF YSLGITFYEL LTGQLPFPSD NPIELIYSHI ARQPPTVHDR
NPEQPRMLSA IVTKLMAKNA EDRYQSPLGL KHDLEQCWSQ WRETGVIHAL ELGTRDWCSR
FLIPEKLYGR EQEVQTLLDA FDRVAHGASE IVLVTGFSGI GKTSVVNEVY PSIVRRRGYF
IQGKFDQFNR NIPLGAFLQI FRNLISQLLS ESDAQLEAWK HKILLVLGKN AQVLIEVVPE
LERILGKQPP ALALSGTTAQ NRFNLLLQKF IQIFAASEHP LVIFLDDLQW IDITSLKLIQ
LLIGEVSKGY ILLIGAYRDN EVFPTHPLIS TLDEIAKTGT ILTRVNLAPL QLDSLNQWIA
DTLNCSPSLA RPLSELVEQK TQGNPFFTAQ FLKALHQAEW ITFDARAGYW QCDITQIREA
ALTDNILELM ALQLQKLPIA TQDLLKLAAC IGNQFDLTTL AIVSEQSEAK ASEQLWPALQ
AGLILPITEV YKFFQNVEAS IPEKTVSEQP VTATYRFLHD RVQQAAYSLI PEDEKQATHF
KIGQLLFHAS TTAAQIEERL FEFLSHLNAG RGLITQPSER QILAQLNLRA GQKAKAATAF
GPAIAYFTAG IDLLPQDAWE QHYDLTLALH EENLEAACLN TDFEHLEPWG DLILQHARSL
LDTIKVYETR MMAARAQGQF RLTLQIGLRA LQLLGVEFSE HPLPTEIEAA AQATRELWAG
PDSSRASPFH LLDLPFVPDP HRSAVMQILS KLGSSVYTVA PDLLPLLSFK LVECSIQGGN
HPISIHAYSG YGMLLCNKFG DIDGGYEFGQ LALTLLEQLQ VKAFKSRVYF VVSALIRHWK
DPLQDLLPYF LDGYQSGLET GDWECVALNA FAYCQLAYLM GQELSDLAGK MEVYHQVICQ
VKQASTLKFH QTYQQAVLNL LGQARVPYRL DGPIYAEEKV LPLLRSTNNH TGLFHTHFNQ
MILCYLFGQY DRAAQQAALA EGSIDAAMGQ FIVALWFFYD ALIHLARYKE ASLTQQAEIL
NRVTTHQTQL KNWASYAPHN HQHRWELVTA ERFAVLGERL QALQHYERAI ESARTHEYFN
DEALANELTA KFYLSWGKEK IAQLYLTEAY YGYVRWGATA KVRDLEQRHP LLLQPKLQPH
PVSLNSLAAT ATTGTLALEA LDLETVLQAS QMLSREIKLD QLLCTLIKLV VQAAGADRGL
LLQPEPTGLW EIIVQLDEHC ACNLQKFPLE GHQDLPQTVV NWVRRTQAAV IENYRLTETQ
FASDPYLIRQ QPQSFLCTPI MSQGKLAAIL YLENRLTGKV FTHDRIEILN LLCTQAAISL
DNARLYQQSE QALVDLRASQ ARFQRVADNL PGVVFQFRLD PDGTPSTPYI STGCMDLYGV
SAEDMMAGIY SLRTFEHPED VAGINQAMET SIQYLTPFHH EWRIIPPSGP VKWIQVASRP
ERQADGAIVW DGVIMDISEK ARLEAERKQA EEALRQMNAE LEFRVEQRTL ELQAAKEAAE
AANRAKSQFL ANMSHELRTP LTAILGFSQI LTHDRALSPQ SRHQVNIINH SGDHLLGLIN
DILEMSKIEA GRVTLTPHPF SLHQLLDTLM EMFYQRAGAK GIQLQCERAL DLPAQIQADE
NKLRQVLINL IGNAVKFTDR GRVVLRVGIE GPATPDTLLF EVEDTGPGIA ASDMEDLFEP
FVQSQSGLKA QEGTGLGLPI SRSFVQLMGG ALTVESRVGW GSIFRFTLPI VRLDESHSAP
HPARRWPIAL APGQPTYRIL IVEDDLASRQ LLLAILEPFG FALQAVTNGQ EALSCWQEWH
PHLIWMDMRM PVMDGYAATQ QIRQQEALLH FPSHTCIIAL TAGVLAEDQS RVLDAGCDDL
VMKPLQETII LDKLAEYLGI CYLYSEDSPS KTELQQEYVF LSPEAQQTLM QSQPISWRRQ
LAHVVIEADI QKLISLIEQI PAQQETLAKW LLQKIDNFDF EHILELTRKA MEE
//