ID A0A2T1G0Y0_9CYAN Unreviewed; 1812 AA.
AC A0A2T1G0Y0;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, 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=C7B67_12785 {ECO:0000313|EMBL:PSB50908.1};
OS filamentous cyanobacterium Phorm 6.
OC Bacteria; Cyanobacteriota.
OX NCBI_TaxID=2107706 {ECO:0000313|EMBL:PSB50908.1, ECO:0000313|Proteomes:UP000239157};
RN [1] {ECO:0000313|Proteomes:UP000239157}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Phorm 6 {ECO:0000313|Proteomes:UP000239157};
RA Moore K., Momper L.;
RL Submitted (FEB-2018) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:PSB50908.1, ECO:0000313|Proteomes:UP000239157}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Phorm 6 {ECO:0000313|EMBL:PSB50908.1,
RC ECO:0000313|Proteomes:UP000239157};
RA Moore K.R., Magnabosco C., Momper L., Gold D.A., Bosak T., Fournier G.P.;
RT "The ancient ancestry and fast evolution of plastids.";
RL Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC Evidence={ECO:0000256|ARBA:ARBA00001433};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.11.1; Evidence={ECO:0000256|ARBA:ARBA00000775};
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:PSB50908.1}.
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DR EMBL; PVWI01000089; PSB50908.1; -; Genomic_DNA.
DR OrthoDB; 9801841at2; -.
DR Proteomes; UP000239157; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd14014; STKc_PknB_like; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.30.450.40; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR041664; AAA_16.
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; IPR000719; Prot_kinase_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
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; PF00069; Pkinase; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00065; GAF; 1.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 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 PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 4: Predicted;
KW Kinase {ECO:0000313|EMBL:PSB50908.1};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000239157};
KW Serine/threonine-protein kinase {ECO:0000313|EMBL:PSB50908.1};
KW Transferase {ECO:0000313|EMBL:PSB50908.1}.
FT DOMAIN 7..274
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 1554..1812
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
SQ SEQUENCE 1812 AA; 202862 MW; 5361397E5063994C CRC64;
MLSLSKYQIN YNLHEGMETI IYRGQKSIDQ PAIILKLLKA EYPTLEAITR LKHEYQIRKH
LDSEQIVKII SLETFDHRLG IVLEDFGGES LGKLIEEEIL SPRAILDIVI QITKALEYLH
QNQIIHKDIK PSNIIINSQT KQVKLTDFGI ATKLNKENPQ FNNPNSVEGT LAYMSPEQTG
RMNRTLDYRT DFYSLGITLY EMLTGTLPFT SNDPLEIVYS HIAIQAISPH QINPKTPQVI
SEIVMKLISK NAESRYQSAA GLLADLENCS HQLETTGKII YFTPGHLDIL SQLLIPQKLY
GRQQQVNQLL AAFERVGASS PESLPPNQNT EKPAHSQSEL MLVSGYSGIG KSAVVNEVSK
PITKAKGYFI SGKFDQFKRN IPYASLIQAF NSLLRQLLTE NAASIETWRT KILTALGTDG
KVIADVIPEV ELIAGKQPEV AELGSVESQN RFNRVFKEFI RVFAQKEHPL VIFLDDLQWA
DSATLKLMQT LITDSEQQYL LLIGAYRDNE VSPTHPLIQT VEEIEKTGTV VNNIVLQPLD
LDNVTELVAE TLNNGTENVK NLAELICNKT GGNPFFLTQL LQALYQDNLL KFDFSLLEGK
GGWNWSIDEI QAIGITDKSV VELVASRIEK LPAATQEVLK LAACVGDKFA LDVLSLVSEE
SANATATELY SALQAGLILP LSDAYRIPLV FDSAESINLK LDTSRVSYKF LHDRVQQAAY
SLIPEDQKQS THLKIGQLLL QNTPPDKLEE NIFDIVNQLN VGIDTISQQS EKTQLAQLNL
TAGRKAKSAA AYEAAVRYLR VAMGLLAEES WQSQYELTLS IYESTAEAEY LNINFEESKK
LIHIILAKAK NILEKVNSYE LYIQSYNAQN RLAEALNTGL EVLRILGISF PQNPNTLNIM
AGLIYTKFSL GTKRVEDLAN LPEMTDPSKQ AIMRILSGIL SSAIQTNPQL LPLLTFMMIQ
HCVKYGNSLY ASIAYVYYGA ILCRLGDINS GYQFGELAIR LLDKFPSRSI KSKVYINFCA
LIKHWKSHLN SVLGYFMETF KAGMETGDLE YAGYAISDYC NYQLWMGEPL YLVEQETGKY
VKLMHKLQLQ MAVPYISIFR QTGLNLCEKA VEPCHLVGES FNEVETLPTL IEAKSFLLVC
MTYNAKAQLN FLFKNYVEAL DNSRLFEKYE EAAAGFYVVS ISNFYYSLSL LALFPQVGKG
EQKQYLKKVI QLQKKMKKWA AHAPMNHQHK YDLVEADKAR VLGQNERAMD YYDRAIDGAA
KNGYIQEEAL AYELAGEFYE SLGKEIISQA YLTKAYYAYI RWGALAKVTD LEFRYPFLVA
QTRTTETRTF DVTRTSTGST TTNGFGNFLD LSAFVKASQA ITSEIVLEKL LTKLINILLE
NAAAQKVVLL LLKNDILCIE ATGNSREDQV TLLPSIPVGN CQDVPLSVIN YVHRSQKHLV
LDNATVAELF NADAYIQKYQ PKSILCLPII YQSQRRGIIY MENALTVGAF TDERVEVLKV
LVSQVAIAVE NAGLYAREQE KSQQLEKSFH ELQEAQLQLI QSEKMSALGN LIAGVAHEIN
NPLGFIAGNV DAAAEASSDL IDYLQLYQEK FPNPGDELED KASEIDLEYL MEDLPKMLLS
MKSGTDRIRN ISTSLRTFSR ADTANKVSTN IHEGIDSTLL ILQYRLKAND TRPAIKIIKE
YGNIPPVKCY FGQLNQVFMN LLANAIDCFE ESNKGRSFAE IELAPNIITI KTEVDAENQT
VFIKMRDNGE GISQEVVSRI FDHLFTTKGV GKGTGLGLSI SRQIVEETHG GCLSCDSVVG
KGTEFAIALP LD
//
