ID U9VZA7_9CYAN Unreviewed; 845 AA.
AC U9VZA7;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=N836_22380 {ECO:0000313|EMBL:ESA33141.1};
OS Leptolyngbya sp. Heron Island J.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Leptolyngbyales; Leptolyngbyaceae;
OC Leptolyngbya group; Leptolyngbya.
OX NCBI_TaxID=1385935 {ECO:0000313|EMBL:ESA33141.1, ECO:0000313|Proteomes:UP000017515};
RN [1] {ECO:0000313|EMBL:ESA33141.1, ECO:0000313|Proteomes:UP000017515}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Heron Island J {ECO:0000313|EMBL:ESA33141.1,
RC ECO:0000313|Proteomes:UP000017515};
RX PubMed=24503993;
RA Paul R., Jinkerson R.E., Buss K., Steel J., Mohr R., Hess W.R., Chen M.,
RA Fromme P.;
RT "Draft Genome Sequence of the Filamentous Cyanobacterium Leptolyngbya sp.
RT Strain Heron Island J, Exhibiting Chromatic Acclimation.";
RL Genome Announc. 2:e01166-e01113(2014).
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: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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:ESA33141.1}.
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DR EMBL; AWNH01000105; ESA33141.1; -; Genomic_DNA.
DR RefSeq; WP_023075909.1; NZ_AWNH01000105.1.
DR AlphaFoldDB; U9VZA7; -.
DR STRING; 1385935.N836_22380; -.
DR PATRIC; fig|1385935.3.peg.6140; -.
DR eggNOG; COG4251; Bacteria.
DR eggNOG; COG4252; Bacteria.
DR OrthoDB; 9809348at2; -.
DR Proteomes; UP000017515; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; 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 Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.40.50.2300; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR InterPro; IPR007890; CHASE2.
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; IPR003661; HisK_dim/P.
DR InterPro; IPR036097; HisK_dim/P_sf.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR PANTHER; PTHR43047:SF79; HISTIDINE KINASE; 1.
DR PANTHER; PTHR43047; TWO-COMPONENT HISTIDINE PROTEIN KINASE; 1.
DR Pfam; PF05226; CHASE2; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM01080; CHASE2; 1.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
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; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils}; Kinase {ECO:0000313|EMBL:ESA33141.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000017515};
KW Transferase {ECO:0000313|EMBL:ESA33141.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..38
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 330..348
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 355..377
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 383..407
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 462..694
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 722..838
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT COILED 410..437
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 771
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 845 AA; 92994 MW; CDBA75081218F950 CRC64;
MWSQQGRRIW KWRLSVISTC SITGLVVGLQ FLGAFQLLEW AALDSCFRLR PPEERDPRIV
IIGISEQDMA EGIGWPLTDA LMAKLINQVA AQNPRAIGLD LYRDVPIEPG HQDLVQVMET
TPQLIGVEKV LDMPVAPPPS LEQKDQVGIA DFVLDADGKI RRGLFSLRTP DNQIKVSLGA
RLALTYLAAE DISLQELNQS LENYQLGNAV LRRFETHDGG YVRADDAGYQ LLLNFRSGSC
TDISLNCPFQ MISKGEFLSG QLPADLLQDR IVLIGATAPS LQDHFYNPYS YGEAISISGV
EVHAHVTSQI ISATLDGRAL IRTWPEPLEY LWILLWSSGG TLLGSLCLNR RRINIGLLWL
IGTLILLLSS LVIGAYLAFL VGWWIPVVPP LMALTGTTVV STTYLLWKNL KLSYRELEQA
NQQLADYSQT LEQKVDARTI DLLVAKETAD QANRTKNDFL ANMSHELRTP LNTILGMTQA
LEEQILGDLN PRQIRALQAT ERSAHHLLEL INDILDLARV ESGVLDLNCA PTAVIPLCHF
CLTIVKQQAH KKGLQLNSKL SHTLPAFVMD ERRIREVLIN LLSNAVKFTP AGGCITLEVV
HQQQPSLSEE TDGSSQDTLK FIVSDTGIGI QPDYIDKLFK PFVQIDSALN RQYAGTGLGL
ALVKRITELH GGTVTVTSEV GIGSTFTVEL PCKAMASPLP SQPPPRLDHQ NLSAADREEL
PTILLVEDDV DNITVFRSYL TAKGYTVCVA NNGHQAISAV LVTVPDLILM DIQMPGMDGL
EAMERIRHQP TSADIPIIAL TALAMKGDRE RCLAAGANEY VSKPVNLGQL VITIEQLLVA
RAPST
//
