ID A0A1Z4JGY9_LEPBY Unreviewed; 1048 AA.
AC A0A1Z4JGY9;
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_28170 {ECO:0000313|EMBL:BAY55990.1};
OS Leptolyngbya boryana NIES-2135.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Leptolyngbyales; Leptolyngbyaceae;
OC Leptolyngbya group; Leptolyngbya.
OX NCBI_TaxID=1973484 {ECO:0000313|EMBL:BAY55990.1, ECO:0000313|Proteomes:UP000217895};
RN [1] {ECO:0000313|EMBL:BAY55990.1, ECO:0000313|Proteomes:UP000217895}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NIES-2135 {ECO:0000313|EMBL:BAY55990.1,
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; BAY55990.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Z4JGY9; -.
DR Proteomes; UP000217895; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR CDD; cd16922; HATPase_EvgS-ArcB-TorS-like; 1.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd00130; PAS; 5.
DR CDD; cd17580; REC_2_DhkD-like; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 2.10.70.100; -; 1.
DR Gene3D; 3.40.50.2300; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 3.30.450.20; PAS domain; 5.
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; IPR001610; PAC.
DR InterPro; IPR000014; PAS.
DR InterPro; IPR000700; PAS-assoc_C.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR013656; PAS_4.
DR InterPro; IPR013767; PAS_fold.
DR InterPro; IPR013655; PAS_fold_3.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR NCBIfam; TIGR00229; sensory_box; 5.
DR PANTHER; PTHR43547:SF2; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE C; 1.
DR PANTHER; PTHR43547; TWO-COMPONENT HISTIDINE KINASE; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF00989; PAS; 1.
DR Pfam; PF08447; PAS_3; 2.
DR Pfam; PF08448; PAS_4; 1.
DR Pfam; PF13426; PAS_9; 1.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00086; PAC; 4.
DR SMART; SM00091; PAS; 5.
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 SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 5.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50113; PAC; 2.
DR PROSITE; PS50112; PAS; 5.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils}; Kinase {ECO:0000313|EMBL:BAY55990.1};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000217895};
KW Transferase {ECO:0000313|EMBL:BAY55990.1}.
FT DOMAIN 20..76
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 168..212
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 285..357
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 434..484
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 487..539
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 540..611
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 616..669
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 694..912
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 934..1047
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT COILED 138..182
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 660..687
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 983
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1048 AA; 117462 MW; 927355E6A66FB763 CRC64;
MTQPRQSLSE FQQFPNSSAD SRYYKQYLET VCNNATLALF VMDEHQQCVY MNPAAEKLTG
YALHELQGRA LHDAIHHTRP DGSPYPLCEC PIDQVFPQNN QEQGEEVFVH RDGHFYPVAY
TASPIREAGQ TIGTVIEVRD ITQEKINAKM QQEVAERERL LREAAEAEKT RAETVLQSIT
DAFIVLDREW NYVYVNAAAT RLFLKSEAEL VGHCIWEVFP EAIHTPIYTE YCRSLAEQKT
IEFECFYSTW NRWFLNRVSP SATGISVFVS DITERKQTQQ ALLESEVRFR SLFECNIIPI
GIWTKDGGLT DGNDALLDLI GYTRAELEAG LLTWKSLTPP EWEKRDAEAV EEIMTRGYCT
AFEKEYIHKN GHRVPILLGG GKFDQASQSG FFFAIDLSQL KQTEAELREA DSLLSSALAA
GSIYTWRWRM QENVISVDAA LAQLLGVDPE TAMRGLPLEI FLNAIHPDDH ESVATAIQTA
IETREDYLTE YRVRSADGSE RWVTARGRVE YDADGTPISF PGALSDITER KQIEATLQET
EERLRLAIES AELGTWDFNL VTGRIIWNDG CKAMFATTGE DEITFDTVQA GMHPDDRDRV
NQFVQAVLAR QSSGDEVIEY RVIGFSDGIE RWVACRGKVF TDSVGNPIRW VGTLLNVTEV
KRREAERQEL LDREKLLREQ AEQANRIKDE FLAVLSHELR TPLNPILGWV KMLKGGKCPP
ERVPQALDTI ERNAVLQAQL IEDLLDVSRI LQGKVVLNGD WINLAETVTA AVETVRLAAE
SKAIELLLTV DPLLGSVRGD ANRLQQVFWN LLSNAVKFTP VSGRVEVTLS QAETEAQIQI
RDSGKGIRAE VLPYIFERFR QADSSTTRQF GGLGLGLAIA RHLVELHGGT ISAESLGENQ
GATFTVRLPI AMIQTQLDQP ERGSEVSQDL LGVKILAIDD EPDNLDFLVF VLEAAGAIVQ
GVQCAKLALE KLSEFSPDLV ISDIAMPDLD GYELIQRVRQ QSDVPAIALT AYAGETNQHQ
ILAAGFQRHL AKPIEPSQVI HEIITLLK
//
