ID A0A0K2LYM5_9NOST Unreviewed; 1255 AA.
AC A0A0K2LYM5;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=AA650_10045 {ECO:0000313|EMBL:ALB40769.1};
OS Anabaena sp. WA102.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Nostocaceae; Anabaena.
OX NCBI_TaxID=1647413 {ECO:0000313|EMBL:ALB40769.1, ECO:0000313|Proteomes:UP000056652};
RN [1] {ECO:0000313|EMBL:ALB40769.1, ECO:0000313|Proteomes:UP000056652}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WA102 {ECO:0000313|EMBL:ALB40769.1,
RC ECO:0000313|Proteomes:UP000056652};
RA Brown N.M.;
RT "The finished genome of an anatoxin-a-producing Anabaena isolate reveals
RT extensive genome rearrangement.";
RL Submitted (MAY-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}.
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DR EMBL; CP011456; ALB40769.1; -; Genomic_DNA.
DR RefSeq; WP_053538908.1; NZ_CP011456.1.
DR AlphaFoldDB; A0A0K2LYM5; -.
DR STRING; 1647413.AA650_10045; -.
DR KEGG; awa:AA650_10045; -.
DR PATRIC; fig|1647413.5.peg.2356; -.
DR OrthoDB; 5389090at2; -.
DR Proteomes; UP000056652; Chromosome.
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; 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; -; 2.
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; 2.
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; 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; 2.
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; 2.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF01627; Hpt; 1.
DR Pfam; PF13426; PAS_9; 2.
DR Pfam; PF00072; Response_reg; 2.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00065; GAF; 2.
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; 2.
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; 2.
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); 2.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50894; HPT; 1.
DR PROSITE; PS50113; PAC; 1.
DR PROSITE; PS50112; PAS; 2.
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 Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 164..235
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 238..290
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 287..325
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 428..564
FT /note="Phytochrome chromophore attachment site"
FT /evidence="ECO:0000259|PROSITE:PS50046"
FT DOMAIN 605..826
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 844..964
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 999..1120
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 1162..1255
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT MOD_RES 897
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 1048
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 1201
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
SQ SEQUENCE 1255 AA; 141249 MW; 4CC7B3594EC85187 CRC64;
MKALLRSDEA GRIEALLQYR ILDTQSELEF DDITRLASFI CGTPMAVMTL VDTDRQWFKS
KIGLEASETP RSIGFCNHAI QQPDPMIIPD ATLDPRFVNN PLVTSDPNIR FYAGIPLIND
EGYGLGALCV LDDIPRQLAP QQIEALNILG RQVMQQLEWR RNLDSLLLST VLDTVNALVI
VLNPEGEIIG FNRACEETTG YSYNEVRNQC FWSVFTEPKR RRTVRSIFEK IKSSKGLKEY
ENYWRIKDGN LRLINWSNRT VLNENGEIEF IVCTGIDITE RKQAEESLKQ QLAAVEAASD
GISIVDKQGN YLYLNSSYVN IFGYSDATEL LGKKWQEVYE QEQIKLFEKK IFPELMKQGY
WHGETIAQRK DSSDFAAEMS LTKLKDGGFI CVGRDISKRK EAEEELKYFN LRSQLLADIT
LKIRGSLQID DILQTSVTEV QKLLKTDRVV ILELLADGSL TARKEALIPG IPVVMGANIV
EPCLTKNYIE KYTQGWIGVI NDIEKANIQP CHIELLQRFN VKANLVIPIF LKDEFWGLLI
AHHCTQPRQW TNWEIEFLKS LSDQIGIALA QAKLLQVEIL QRRELEIARH QAELASLSKS
SFLANMSHEI RTPMNGILGM TGLLLETPLN PEQRDFLEIV RVSGDALLSL INEILDLSKL
EAGEMMIESI DFDLCNCLEE VLDLLAPQAH QKGLEIATLV EQNVYKYLRG DVGRLRQIIM
NLIGNAIKFT KEGEVLLEVE LRSETQDLVI LNFTVIDTGI GISLQDQNKL FQAFSQVDAS
ITRQYGGTGL GLAICQQLVS LMGGKIGVKS QLGKGSQFWF ELPFMKQIHP SSQILELDIL
TNKRLLVIDD NGTNRRIIYH QATHWGMWVD EAACANTGLA ALQKAAENHP YDIVIIDMQM
PAIDGLTLGS QIKANSAISN IPLVLLTSSN QKDEWKKAIN IGFISYLVKP IKPSRLLDTI
MDILANQPKL DNFQSSKIEQ SSITVLDEKI SDSTTSKLKL LVAEDNPVNQ KVILKQLDSL
GYKADIVANG QEVLEMLDNI AYDLILMDCQ MPILDGLKTT KVIRSRPISS FVNHRQPIVI
AITANAMKED QQNCLDAGMD DYFSKPITKD KLATLLELWS SRIIAGRVVT IPESEPVVLI
TNNPLTDLPI DWEHLHQISE NDPEFELEIL KVFVEDSLFH VEGIKAAIAV NDFPQLAREA
HHLKGSSGNI GTTAIQKIAE ELEQLSRKQS FVGAYELLLE LVDFINKIQA FLTKS
//
