ID F4LNT0_TREBD Unreviewed; 696 AA.
AC F4LNT0;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 27-MAR-2024, entry version 67.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN OrderedLocusNames=Trebr_1491 {ECO:0000313|EMBL:AEE16915.1};
OS Treponema brennaborense (strain DSM 12168 / CIP 105900 / DD5/3).
OC Bacteria; Spirochaetota; Spirochaetia; Spirochaetales; Treponemataceae;
OC Treponema.
OX NCBI_TaxID=906968 {ECO:0000313|EMBL:AEE16915.1, ECO:0000313|Proteomes:UP000006546};
RN [1] {ECO:0000313|Proteomes:UP000006546}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 12168 / CIP 105900 / DD5/3
RC {ECO:0000313|Proteomes:UP000006546};
RA Lucas S., Han J., Lapidus A., Bruce D., Goodwin L., Pitluck S., Peters L.,
RA Kyrpides N., Mavromatis K., Ivanova N., Mikhailova N., Pagani I.,
RA Teshima H., Detter J.C., Tapia R., Han C., Land M., Hauser L.,
RA Markowitz V., Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Gronow S.,
RA Wellnitz S., Brambilla E., Klenk H.-P., Eisen J.A.;
RT "The complete genome of Treponema brennaborense DSM 12168.";
RL Submitted (APR-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; CP002696; AEE16915.1; -; Genomic_DNA.
DR AlphaFoldDB; F4LNT0; -.
DR STRING; 906968.Trebr_1491; -.
DR KEGG; tbe:Trebr_1491; -.
DR eggNOG; COG0643; Bacteria.
DR HOGENOM; CLU_000650_2_1_12; -.
DR OrthoDB; 9803176at2; -.
DR Proteomes; UP000006546; Chromosome.
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; 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; 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:SF8; HISTIDINE KINASE; 1.
DR PANTHER; PTHR43395; SENSOR HISTIDINE KINASE CHEA; 1.
DR Pfam; PF01584; CheW; 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; 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:AEE16915.1};
KW Phosphoprotein {ECO:0000256|PROSITE-ProRule:PRU00169};
KW Reference proteome {ECO:0000313|Proteomes:UP000006546};
KW Transferase {ECO:0000313|EMBL:AEE16915.1}.
FT DOMAIN 7..111
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT DOMAIN 276..419
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 421..557
FT /note="CheW-like"
FT /evidence="ECO:0000259|PROSITE:PS50851"
FT DOMAIN 576..692
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT MOD_RES 54
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
FT MOD_RES 625
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 696 AA; 78780 MW; 05396BBB4DA9AF98 CRC64;
MERVKANLMD TENFIQDYLV EAREYLDSLD DFCIRVGKND RDEELLKELL RILHTFKGTS
RIMGFSKVEQ IIHGMETVFK NIQSNHVEIK KSEISLLLSV VSVVRKAVDS IEVSGVENIP
CFDSAVENIR RASCGDDFSA DFAPGKKTAD GGDEDATVFH DSQTIKINVA QINDILQLFD
KLIMRQIRLK NEISDVKSKC SAGDNLFREV DENMEVLEKQ SFNIQERIIA LRMLPFDMML
QPLKHSVAQE AAKLGKDVDF DIPCSEITID KTILERLPKI LVHLVRNAID HGIEDAEDRE
SLGKPSKGYV RITVHQKSSR VVVTVSDDGR GIDFEKIRST AKVRYPEREK EIEKMEKNDL
IQFLFESGFS TRDTVSELSG RGVGMDVVRS EMDRLKGKIS ITSDRHKGTA IELVLPFSLA
TQDGLFIRQG KNTYLVLSHY VKEILTVPRS SFLMMQKGPV VNLHNELVPL YDFDAIIGNL
SGTYALSDAE VPVIVIEYLN RKIAVMLDEV LYYKTVVIKP VPPLLKNVEG LQGVVFDENY
RIIPVLNIPN CMERFRSLSI YSEKELEVKK TAKVRSVLIV DDSHTTRNIE KIILESEHYA
VDTACDGIEA LEKLKGRRFD LVVTDIKMPR MDGFVLLHNM RHTAEFSDIP VIVVSSVFES
DTAAKVSKMG AQGYIVKSDF ERENLIEKAK ELLSHG
//
