ID H2C9Z2_9LEPT Unreviewed; 1071 AA.
AC H2C9Z2;
DT 21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT 21-MAR-2012, sequence version 1.
DT 27-MAR-2024, entry version 62.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=Lepil_0410 {ECO:0000313|EMBL:EHQ05116.1};
OS Leptonema illini DSM 21528.
OC Bacteria; Spirochaetota; Spirochaetia; Leptospirales; Leptospiraceae;
OC Leptonema.
OX NCBI_TaxID=929563 {ECO:0000313|EMBL:EHQ05116.1, ECO:0000313|Proteomes:UP000005737};
RN [1] {ECO:0000313|EMBL:EHQ05116.1, ECO:0000313|Proteomes:UP000005737}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 21528 {ECO:0000313|EMBL:EHQ05116.1,
RC ECO:0000313|Proteomes:UP000005737};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Peters L., Mikhailova N., Held B.,
RA Kyrpides N., Mavromatis K., Ivanova N., Markowitz V., Cheng J.-F.,
RA Hugenholtz P., Woyke T., Wu D., Gronow S., Wellnitz S., Brambilla E.-M.,
RA Klenk H.-P., Eisen J.A.;
RT "The Improved High-Quality Draft genome of Leptonema illini DSM 21528.";
RL Submitted (OCT-2011) 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; JH597773; EHQ05116.1; -; Genomic_DNA.
DR RefSeq; WP_002769457.1; NZ_JH597773.1.
DR AlphaFoldDB; H2C9Z2; -.
DR STRING; 183.GCA_002009735_00002; -.
DR HOGENOM; CLU_287562_0_0_12; -.
DR Proteomes; UP000005737; Unassembled WGS sequence.
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; cd00082; HisKA; 1.
DR CDD; cd00130; PAS; 5.
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; 3.30.450.20; PAS domain; 5.
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; 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; IPR004358; Sig_transdc_His_kin-like_C.
DR NCBIfam; TIGR00229; sensory_box; 4.
DR PANTHER; PTHR43304:SF1; PAC DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR43304; PHYTOCHROME-LIKE PROTEIN CPH1; 1.
DR Pfam; PF01590; GAF; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF00989; PAS; 2.
DR Pfam; PF08448; PAS_4; 2.
DR Pfam; PF13426; PAS_9; 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 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; SSF55785; PYP-like sensor domain (PAS domain); 5.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50113; PAC; 4.
DR PROSITE; PS50112; PAS; 5.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils}; Kinase {ECO:0000313|EMBL:EHQ05116.1};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000005737};
KW Transferase {ECO:0000313|EMBL:EHQ05116.1}.
FT DOMAIN 1..64
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 275..346
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 349..401
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 416..486
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 489..541
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 556..626
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 625..681
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 696..750
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 765..821
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 857..1070
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT COILED 812..850
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 1071 AA; 121898 MW; FB63FA9859B4AD3F CRC64;
MEFQIRTALG VLDQDLRLSD ADTRLCEILG IESNSVQGCP FEQFLPDESK TDFRRAVTHA
LRDGSHETSI TLQNGDGSYV FVADMQLRRL AAYTILIQVV DSTRARRIEG SIRSLARETA
PLTGQAFFDS VTELLAEATG MRIAFVGRRI ANDRIRTISV WDDARGGRVD DFEYELKGSP
CETVVANDPC FFCDSVCRRF PEDALLQQMQ MESYQGIPVH SVAGELLGII VLLHDRPMEP
IPELDPTLTL LAARAGAEME RMESERALLE QLAADQNYMS TILETTGALI IVVDRDGNII
TFNRGCEETS GYSREEVTGQ PFWKYLIPED ERPAVIEALK SLSAGHFPAT FENHWLRRDG
TKRWISWSNT CTLKPDGSVD LVIGTGIDIT EKKEMQHDLL QANEELAEQL GAVDQERNLR
KQIMETSGAI VLVVDEEGRL IEFNSAAEQA TGYERTEVIG QSATLLVPEK LRTVTLAGLK
ERLAAGTDSS SEYILLRKDG QKRWVTWQNS VYREPLLGRR LLISIGIDIT ERKKFEEEQQ
QLFKQIERTF QEIVRERNFR QQILDTAAAI ICVADTDGNV IEFNRVAEEI SGYTKDELLG
KPYFILLPPD QRDSARNRLK QMEDGDVEHN IVYPWLTRSG DERHILWSNS AFFDRQGGME
FVIGTGIDIT ERVEVERVRE ELFERLQHSL QELQREREFR QSIVETSSAL IIVLSETGQI
IEFNRGCEEV SGYRRDEVIG RHFSFLIPVD EGHHVMNRFA EMPLKEIEPN VENGWLTKSG
DIRWILWNNS SVTDPQTGQQ IIIGTGIDIT ERKKAQKELA EAYEDLKLLN DHLEDRVRER
TMQLQAANQE LEAFSYSVSH DLRAPLRHIT GFIDLIHMKA FELDPQLRKY LDIIADSAKR
MGMLIDDLLQ FSRMGRTEMS QSVIDLNGIV TRVINDLSYE TQGRNIDWRI TELPRMRCDP
SMILLVFQNL IGNALKFTRN RDPAVIEIFS EQAEKGTTIH VRDNGVGFDM QYADKLFGVF
QRLHRAEEFE GTGIGLANVR RIVHRHGGTV HVVAALNEGA DFSFHLPELR S
//
