ID A0A2T1G3T6_9CYAN Unreviewed; 988 AA.
AC A0A2T1G3T6;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=C7B67_09440 {ECO:0000313|EMBL:PSB51830.1};
OS filamentous cyanobacterium Phorm 6.
OC Bacteria; Cyanobacteriota.
OX NCBI_TaxID=2107706 {ECO:0000313|EMBL:PSB51830.1, 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:PSB51830.1, ECO:0000313|Proteomes:UP000239157}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Phorm 6 {ECO:0000313|EMBL:PSB51830.1,
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 + 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:PSB51830.1}.
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DR EMBL; PVWI01000058; PSB51830.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2T1G3T6; -.
DR OrthoDB; 2079555at2; -.
DR Proteomes; UP000239157; Unassembled WGS sequence.
DR GO; GO:0004673; F:protein histidine kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0006935; P:chemotaxis; IEA:InterPro.
DR GO; GO:0000160; P:phosphorelay signal transduction system; IEA:InterPro.
DR CDD; cd16916; HATPase_CheA-like; 1.
DR CDD; cd00088; HPT; 2.
DR Gene3D; 3.40.50.2300; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 1.20.120.160; HPT domain; 2.
DR Gene3D; 2.30.30.40; SH3 Domains; 1.
DR InterPro; IPR036061; CheW-like_dom_sf.
DR InterPro; IPR002545; CheW-lke_dom.
DR InterPro; IPR011006; CheY-like_superfamily.
DR InterPro; IPR003594; HATPase_C.
DR InterPro; IPR036890; HATPase_C_sf.
DR InterPro; IPR005467; His_kinase_dom.
DR InterPro; IPR036641; HPT_dom_sf.
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 PANTHER; PTHR43395:SF1; CHEMOTAXIS PROTEIN CHEA; 1.
DR PANTHER; PTHR43395; SENSOR HISTIDINE KINASE CHEA; 1.
DR Pfam; PF01584; CheW; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF01627; Hpt; 2.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00260; CheW; 1.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00073; HPT; 2.
DR SMART; SM00448; REC; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF50341; CheW-like; 1.
DR SUPFAM; SSF52172; CheY-like; 1.
DR SUPFAM; SSF47226; Histidine-containing phosphotransfer domain, HPT domain; 2.
DR PROSITE; PS50851; CHEW; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50894; HPT; 2.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Kinase {ECO:0000313|EMBL:PSB51830.1};
KW Phosphoprotein {ECO:0000256|PROSITE-ProRule:PRU00169};
KW Reference proteome {ECO:0000313|Proteomes:UP000239157};
KW Transferase {ECO:0000313|EMBL:PSB51830.1}.
FT DOMAIN 1..104
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT DOMAIN 200..304
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT DOMAIN 570..708
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 710..844
FT /note="CheW-like"
FT /evidence="ECO:0000259|PROSITE:PS50851"
FT DOMAIN 868..984
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT MOD_RES 46
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
FT MOD_RES 247
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
FT MOD_RES 917
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 988 AA; 109134 MW; F3C654CF34E782DD CRC64;
MSNFSMMDLF RMEADSQVEI LNENILALEN NPSSPAELES LMRAAHSLKG AARIVGLDAA
VRVAHVMEDC FVAAQAGAIA LDAPDKIDVM LRAIDLLAQI SQIPETEIEN WLPFNRSQIE
SLETAILAII NNEKLDIGSQ SEAEQIEPET IFESQITPEL AAQFYLDFTI ETTDYPQSNS
DIFQKILPEL PKLESPETRL LKTDLPMLAL FLAEVEAQSI LLNQTLLALK NNPNEYLDLD
SLIKSAHLIK GAARIVQFNQ VIKLAWAIED TFVALQKYKA SLNVSQIDSL LFGVNILENM
QKIPVLEIEN WLEEGDEKID RIVAAINLIS EATKIQKVAI SANKTNSQIT PTAQPQLQNT
TAELTESSGQ ISQTSNSTAV TVEQLSTQRA IGKTATANLR ENAQKPKTAD RVVRVNAENL
NRIMGLAGES LVEAKWLQPF ADSLLKLRTH QGQLYSLLEK LQESLGDSVL DQRSEDYLGS
ARKKANDCRH ILSDRLNELE LFARRSANLS DRLYREVIAS NMRPFADGVP AFPRMLRDLA
RQLGKQVKFE VVGKSTQVDR DILEKLEAPL THILRNALDH GIEAPEPRLA AGKPAEGTIR
LEAAHRGGML SITVSDDGSG IEPEKLREKI VTKGMVSAEM AAKLTEPELM DFLFLPGFST
ASQVTEISGR GVGLDIVQSM VQEVGGILRA TSLPGKGMSF HLQLPLTLSV IRTLLVEISG
EPYAFPLTRI DRILMVDTAE IAIAENRQYF TLDNQNIGLV TAYQVLQLPA PSHKLDFLPV
IIVSDRSSSY GLAVDKFLGE RDLVVRPLDP RLGKVADISA AAFMEDGAPV LIIDVEDLVR
STDKLLTESR LQKVSQTAQT AESTTRKRVL VVDDSITVRE VERKLLENQG YEVEIAVNGM
DGWNALRTGN FDLVISDVDM PRMTGIELVS QIKNHSGLKS IPVIIVSYKD REEDRIRGLE
VGADYYLTKS SFHDDTLLNA VVDLIGEA
//
