ID A0A1E5QNW2_9CYAN Unreviewed; 1594 AA.
AC A0A1E5QNW2;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 24-JAN-2024, entry version 31.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=BH720_05485 {ECO:0000313|EMBL:OEJ76287.1};
OS Desertifilum tharense IPPAS B-1220.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Desertifilales; Desertifilaceae;
OC Desertifilum.
OX NCBI_TaxID=1781255 {ECO:0000313|EMBL:OEJ76287.1, ECO:0000313|Proteomes:UP000095472};
RN [1] {ECO:0000313|EMBL:OEJ76287.1, ECO:0000313|Proteomes:UP000095472}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IPPAS B-1220 {ECO:0000313|EMBL:OEJ76287.1,
RC ECO:0000313|Proteomes:UP000095472};
RA Sinetova M.A., Bolakhan K., Zayadan B.K., Mironov K.S., Ustinova V.,
RA Kupriyanova E.V., Sidorov R.A., Skrypnik A.N., Gogoleva N.E., Gogolev Y.V.,
RA Los D.A.;
RT "Draft genome of thermotolerant cyanobacterium Desertifilum sp. strain
RT IPPAS B-1220.";
RL Submitted (SEP-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:OEJ76287.1}.
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DR EMBL; MJGC01000040; OEJ76287.1; -; Genomic_DNA.
DR RefSeq; WP_069966163.1; NZ_MJGC01000040.1.
DR STRING; 1781255.BH720_05485; -.
DR OrthoDB; 9809348at2; -.
DR Proteomes; UP000095472; 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; 3.
DR CDD; cd17546; REC_hyHK_CKI1_RcsC-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; 3.30.450.20; PAS domain; 7.
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; IPR013655; PAS_fold_3.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR NCBIfam; TIGR00229; sensory_box; 4.
DR PANTHER; PTHR45339; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE J; 1.
DR PANTHER; PTHR45339:SF1; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE J; 1.
DR Pfam; PF01590; GAF; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF08447; PAS_3; 3.
DR Pfam; PF08448; PAS_4; 3.
DR Pfam; PF13188; PAS_8; 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; SM00086; PAC; 6.
DR SMART; SM00091; PAS; 7.
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); 7.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50113; PAC; 4.
DR PROSITE; PS50112; PAS; 4.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
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:UP000095472};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 171..211
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 382..433
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 434..504
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 507..559
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 722..796
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 798..850
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 971..1017
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 1046..1098
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 1116..1358
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 1384..1503
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT MOD_RES 1433
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1594 AA; 179514 MW; 97BDD649444C2C60 CRC64;
MHSRNPEPPS SKPFDLATLI QLQSKIASEI ELHQLLITLI GILIETVEAQ SGYILLEKDG
EFKIEAAKSA RSHQVEVLRS LPLKRRVSLA AIEQATRSRT PILSTIQQRQ AKSVLCCPLL
HQERPIGFIY LEKSLKPSPF TEQDKERIQL LAIPAAIALQ AAQRYAEVQA TQSRLQKFLD
AIPIGISIHD RSGQIVYANR ASRKILNLHQ QLPLSEVETL SQVFQVYRVG TQEPYPVEEL
PLVKAFAGKT ASADDLELHQ AHRQIPLEVK SMPVWGEDGR VEYAIAAFQD ISARLNAQNA
LRESETKFRN LAENSPGMIY RYIIHPDGSD RIAYLSSRCR EICEIDPEVA LQNPRTIENF
IPLEELSRIR YAFSSSVKPQ QWSKEYCIIT PSGQQKWVQN SATFERHSNG DLIWDGLILD
ITQRKHAELA LFESEQRYAN LTQIAPVGIF RNNAEGLCVY GNERSFEMIG LSPTEALGFG
WTKTLHPDDR DRVTAAWEKF MAEQSDFACE YRFLRPDGSE IWVFGQAAIE RDRAGKMTGT
IGTLTDITAA KRVEAALRES EAKFRHLAEN VPGAIYRYVL HPDGSHAFTY ASPRIQEFYD
ASPADLLQNA DLAWQKTHPD DLAFLNESIR ISATTLQPWR WEGQVVSKQG LRWVQGISQP
EKQPNGDIVW DGLLLDITER KRVEQLVADY NWNLSQQVQE RTVALEQQIK ERLQVEAALR
ENEQKFRAIF DQAFQFVGLL QPDGMMLEAN QTALAFAGVS REQVVGQPFW DSPWWKFSPE
AQAKLKTAIA QAAQGAFIRY EAEVWGADNR LVTIDFSLRP LLNEAGEVVM LIPEGRDISD
RKQAEAALQQ SEATLRQILE ALPDLVILMD RQGYQLEQLN GGIFKSIVTR EEGVGKSIFD
FLPQPLARRR LAALQTALDK GETQVYQQEI VVEGEARYEE VRILPVSQDT ALVIIRDVSD
RAIAEMELRS QQAFLRQVID VVPSSIFVKD REGRFLTINQ SGAAIYGLPI EEMIGKTDYD
LNPNTAQVDE FLAINRAVME TLQPYITPAE AIVNRQGEQR WYQTIVSAFI DADGEVQGII
GSATDISTIK QVEEELRVAK EAAEAANRAK SIFLANMSHE LRTPLNAILG FSQLMYQAKN
LSGEQQENLN IIRRSGEHLL TLINQVLDLS KIEAGRMTLN ANSFDLSRLL EDIEDMFSLR
TQDKGIHLRF STCSDVPQYV QADEIKLRQV LINLLSNAVK FTAQGGVQLQ VRVVEHLDPA
KVRLQFQVSD TGVGIPPEEL PHLFKPFIQT SSGQQVQEGT GLGLCISYQF VLMMGGEMTA
ISRGKAFNPS RGDAVEKRQD NGSVALGTTF EFEIPVSMAI ATQIPAADRG RRAIAIAPHQ
PQYRFLIADD NNYNRQLLLK LLQPFGFELQ VVTNGSDALE RWKSWHPHLI WMDIRMPVMD
GCTATRQIRQ AEQQTQQAPC KIIALTASAL AGEKALVLNS GCDDFIRKPF QDNEIVEAIH
RHLGVMFIYE ADREHPAAPH SEPMSLNPND LTGLPIDWLL ELYQAVIEGD LEEITAHLDK
IKPEFQEIAN AISQLADRYQ FEQILNLIQA VNNL
//
