ID A0A0D8ZNK5_9CYAN Unreviewed; 1788 AA.
AC A0A0D8ZNK5;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 27-MAR-2024, entry version 46.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=UH38_21115 {ECO:0000313|EMBL:KJH69932.1};
OS Aliterella atlantica CENA595.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Chroococcidiopsidales;
OC Aliterellaceae; Aliterella.
OX NCBI_TaxID=1618023 {ECO:0000313|EMBL:KJH69932.1, ECO:0000313|Proteomes:UP000032452};
RN [1] {ECO:0000313|EMBL:KJH69932.1, ECO:0000313|Proteomes:UP000032452}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CENA595 {ECO:0000313|EMBL:KJH69932.1,
RC ECO:0000313|Proteomes:UP000032452};
RA Rigonato J., Alvarenga D.O., Branco L.H., Varani A.M., Brandini F.P.,
RA Fiore M.F.;
RT "Draft genome of a novel marine cyanobacterium (Chroococcales) isolated
RT from South Atlantic Ocean.";
RL Submitted (FEB-2015) 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 -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000256|ARBA:ARBA00004429}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004429}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
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:KJH69932.1}.
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DR EMBL; JYON01000031; KJH69932.1; -; Genomic_DNA.
DR RefSeq; WP_045056670.1; NZ_JYON01000031.1.
DR STRING; 1618023.UH38_21115; -.
DR PATRIC; fig|1618023.3.peg.2520; -.
DR OrthoDB; 5389090at2; -.
DR Proteomes; UP000032452; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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; cd19410; HK9-like_sensor; 1.
DR CDD; cd00088; HPT; 1.
DR CDD; cd00130; PAS; 2.
DR CDD; cd17546; REC_hyHK_CKI1_RcsC-like; 2.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.30.450.40; -; 3.
DR Gene3D; 3.40.50.2300; -; 2.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 1.20.120.160; HPT domain; 1.
DR Gene3D; 3.30.450.20; PAS domain; 3.
DR InterPro; IPR007891; CHASE3.
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; IPR036641; HPT_dom_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; IPR016132; Phyto_chromo_attachment.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR008207; Sig_transdc_His_kin_Hpt_dom.
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; PF05227; CHASE3; 1.
DR Pfam; PF01590; GAF; 2.
DR Pfam; PF13185; GAF_2; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF01627; Hpt; 1.
DR Pfam; PF08448; PAS_4; 1.
DR Pfam; PF13426; PAS_9; 2.
DR Pfam; PF00072; Response_reg; 2.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00065; GAF; 3.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00073; HPT; 1.
DR SMART; SM00086; PAC; 2.
DR SMART; SM00091; PAS; 3.
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; 3.
DR SUPFAM; SSF47226; Histidine-containing phosphotransfer domain, HPT domain; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 3.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50894; HPT; 1.
DR PROSITE; PS50113; PAC; 2.
DR PROSITE; PS50112; PAS; 3.
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 Cell inner membrane {ECO:0000256|ARBA:ARBA00022519};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000032452};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 187..206
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 361..382
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 399..470
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 473..525
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 694..740
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 783..835
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 836..882
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 980..1115
FT /note="Phytochrome chromophore attachment site"
FT /evidence="ECO:0000259|PROSITE:PS50046"
FT DOMAIN 1156..1377
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 1395..1515
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 1539..1661
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 1695..1788
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT COILED 212..239
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1109..1146
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 1449
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 1589
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 1734
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
SQ SEQUENCE 1788 AA; 198813 MW; 98DD9F692D4632C1 CRC64;
MTLLPDNEAQ RIEALLQYKI LDTPAEAAFD DLTQLASYIC GTPVALINLV DRDRLWIKSN
TGLGSLNEVP RDIAFCAHTI LQPDVLMVPN TATDDRFATN PLVTSDPKFR FYTGVPLHNP
EGHALGTLCT LDYIPRELTP EQLEALRLIG RQVVKQLEMR RNLANLTLVT ASERKTEKTR
QQFFKKIAGG FCITSLILLA VSLVSYRSIT KLIDINQQVQ TSEEKINALE EVLSQLKDAE
TGQRGYLITA DGNYLAPYSS ASLEVNQELQ IIRNLTANNP KQQQQLNLLE PLVAQKLAEL
KTTIDLRREQ GLEAALQVVK TNQGKQLMDD IRQIIAQMKQ QEKALLAQHS AAARASARNT
ILVLAIALLL VLTLLAALYY LIYSEFTERK QIEIALKKER NFISAIIDTA SALVVVLDAQ
GKIVRFNSSC EQTTGYSFDE VRDRYFWDLF LIGEELEAVK NLFTQLSQTK FPNEHENYWR
TKDGNRRRIA WSNSALFNNQ GEVEYIISTG IDISERKRAE QRLLVQHAVT RILAESDTLG
IVTPKILQAI CQNLEWELGE LWSVEAQANV LQCLKTWHLP SIDITNFGQV TQAIAFAPGV
GLPGRVWASI QPVWISDLSC DANFHRTKVA LESGLHSAFG FPIHSGSDFL GAMVFFSRKS
QQPDPELLEM MAAIGSQIGQ FMKRKQAEVA LQHTTTLQRA ILDSANYAIV STELDGTITT
FNAAAQKALG YSSQKVIGKT TPAIFHDWSE VEQRAEELSQ ELGITIEPGF EVLVAKARHG
EIEEREWSFI RQDGSKFPVM LSVTALRDSN DNITGFIAIA SDITQRKQAL LALQSSEERF
QTFMNNSPVI AFIKDEEGRY VYVNEPLESA FNISSADLLG KTDFDWLPLK VANQVRHNDL
TVFSTEKTCQ AIESVTLADG CLHHWLVLKF LIKDSSDRPM LGGVGIDITE RKQAEEALNL
QNLRSQLFTE ITLKLRQSLQ VADILQTTVA EVQKILSCDR VLVYQLGSSN AGTIVTEAVA
PGCNAMQGQS INHGNFGEVY NIYRQGKGLA IADLDASNLQ HSYKQMLQRN GVKANLVMPI
LLKGELWGLL IAHQCDRPRQ WTDFEFDLLQ QLADQVAIAL TQAQLLQAET QQRQELEIAR
RQAELASQTK SNFLANMSHE IRTPMNAILG MTGLILETSL TPEQRDFMET VRISGDALLS
LINEILDLSK LEAGEMVLDK YNFDLSTCVE EVLELLAPQA HNKGLEIAAL IYRNVPTHLQ
GDAGRLRQIF MNLIGNAIKF TSQGEVVVRA ELRSETATTA KIRFAISDTG LGIAPEDRDK
LFSPFIQVDA STTRKFGGTG LGLAICKQLV TLMQGEIGLE SELGIGSKFW FEVTFSKQLQ
PVVNVNDCSL LANKRLLVVD DNVTNRTIVN YQATRWGMQV GEADSASAAM VALQQAKGQN
LPYDLVAIDM QMPEVDGITL GAQIRASGFA DLPLIMLTST NQRDEVKNAL DVGFAAYLVK
PVKPSRLFDT IVNILGSPEI EPQIQQIEAV PSQSQSSLRI LLAEDNLVNQ KVAIKQLKSI
GYEPADIAAN GQEVLQLLKE VAYDLILMDC QMPVLDGLEA TREIRQWDES CFVNGTRPVI
IAVTANAMTE DKQRCLDAGM DDYLSKPVIK AELAAIIERW ANTIFAKKSP VAQVDAVDTA
LPIDWETLHQ LSDGDRDFEI ELLQMLVEDM QVHVAATKDA IASSDFTQVG REAHHLKGVT
GNIGAKTMYQ AAIKLEEIAL NQERRGTGDL LAKFENFINS VQNYLQEQ
//
