ID A0A1Z4JQB6_LEPBY Unreviewed; 963 AA.
AC A0A1Z4JQB6;
DT 27-SEP-2017, integrated into UniProtKB/TrEMBL.
DT 27-SEP-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=NIES2135_58460 {ECO:0000313|EMBL:BAY58971.1};
OS Leptolyngbya boryana NIES-2135.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Leptolyngbyales; Leptolyngbyaceae;
OC Leptolyngbya group; Leptolyngbya.
OX NCBI_TaxID=1973484 {ECO:0000313|EMBL:BAY58971.1, ECO:0000313|Proteomes:UP000217895};
RN [1] {ECO:0000313|EMBL:BAY58971.1, ECO:0000313|Proteomes:UP000217895}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NIES-2135 {ECO:0000313|EMBL:BAY58971.1,
RC ECO:0000313|Proteomes:UP000217895};
RA Hirose Y., Shimura Y., Fujisawa T., Nakamura Y., Kawachi M.;
RT "Genome sequencing of cyanobaciteial culture collection at National
RT Institute for Environmental Studies (NIES).";
RL Submitted (JUN-2017) 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};
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DR EMBL; AP018203; BAY58971.1; -; Genomic_DNA.
DR RefSeq; WP_017290595.1; NZ_AP018203.1.
DR AlphaFoldDB; A0A1Z4JQB6; -.
DR Proteomes; UP000217895; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR GO; GO:0006935; P:chemotaxis; IEA:InterPro.
DR CDD; cd00088; HPT; 1.
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; 1.
DR Gene3D; 2.30.30.40; SH3 Domains; 1.
DR InterPro; IPR004105; CheA-like_dim.
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; PF02895; H-kinase_dim; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF01627; Hpt; 1.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00260; CheW; 1.
DR SMART; SM01231; H-kinase_dim; 1.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00073; HPT; 1.
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; 1.
DR PROSITE; PS50851; CHEW; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50894; HPT; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Kinase {ECO:0000313|EMBL:BAY58971.1};
KW Phosphoprotein {ECO:0000256|PROSITE-ProRule:PRU00169};
KW Reference proteome {ECO:0000313|Proteomes:UP000217895};
KW Transferase {ECO:0000313|EMBL:BAY58971.1}.
FT DOMAIN 2..107
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT DOMAIN 428..662
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 664..806
FT /note="CheW-like"
FT /evidence="ECO:0000259|PROSITE:PS50851"
FT DOMAIN 840..957
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT MOD_RES 49
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
FT MOD_RES 890
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 963 AA; 106648 MW; D4E18F85C31BD59C CRC64;
MAQDKELEIR RQFLDEAQEY LDVLDATILD LANHPIDVAK ANAALRAAHS IKGGAGMMGF
QVLSELAHRL EDSWKVLKID KSIVVSPRLE NLLLASVGCL RQVVEFDRES MQRHQDSFVD
ANWLSVEAYP VFDALHAELG DPQEENAASI LSPEEGQDIV PLLFETEVEG CLERLETVLN
TPDQPCLREE VAILAQELGG LGEMLQLSQF VQLCQSIAYA IEQDSQNTSA IAESALTAWR
TAQKLAIAGQ YDQIPTAIAE STLPPDLADF ADVPSVLEPN VGETDWFTEA LAAEALAVDD
FQPIPMPTRI PVGEPKGTDF KILDPEPDIS TATEAQDTTV RVPVRQLNQL NDSFGELTID
RNGLDLYLKR LRGLARTLHD RVQVLDQVNA KLRTAYDRVT LDGSRSLQDN RRSGFDALEL
DRYGDLHLLS QQVMETIVQL QEVSEDIDLS LDDADQSARN LTKTAKQLQS GLTQLRMRPI
SDVINRFPRA IREWSLQYGK EVQLSVVGGS TLIDRNLLEA LNDPLMHLIR NAFDHGIEEP
TLRALRGKPP QGTIEIQAAN QGNRTIITVR DDGEGIPIDK IRDRAEQMGL DPVLLDAARD
EELLSLIFEP GFSTSTQVTA LSGRGVGMDV VRNNLKQIRG EISVNTQAGQ GTTFTLSIPF
ALSTIKVLLI ECHGMLLALP TDVVSELFLL QPNQIIETAG SEVLNWQDKV VQLVRLQKWM
RFNCPQIPHG FETPPTIAMT SVVIIDQAPQ WFGIQIDRCW GEQEATMRKV EGNLALPTGF
SGCTILGDGR VVPLVNVTEL LRWITSCERS DIQPDQAFSK QLRASLVASQ PSMARSTTPT
ILVVDDSINV RRFLALTLER SGYRVEQAKD GQDAIERLEA GLSVQAVICD IEMPRLDGYG
FLAKLRSDEQ LAQIPVMMLT SRSGEKHRKV AENLGAAAYF SKPYNEQVLL RTLEGMVKST
ALV
//
