ID F4LLD6_TREBD Unreviewed; 586 AA.
AC F4LLD6;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, 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 OrderedLocusNames=Trebr_0163 {ECO:0000313|EMBL:AEE15614.1};
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:AEE15614.1, 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; AEE15614.1; -; Genomic_DNA.
DR RefSeq; WP_013757333.1; NC_015500.1.
DR AlphaFoldDB; F4LLD6; -.
DR STRING; 906968.Trebr_0163; -.
DR KEGG; tbe:Trebr_0163; -.
DR eggNOG; COG2205; Bacteria.
DR HOGENOM; CLU_463749_0_0_12; -.
DR OrthoDB; 9813151at2; -.
DR Proteomes; UP000006546; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd00082; HisKA; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
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 PANTHER; PTHR45453; PHOSPHATE REGULON SENSOR PROTEIN PHOR; 1.
DR PANTHER; PTHR45453:SF1; PHOSPHATE REGULON SENSOR PROTEIN PHOR; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
PE 4: Predicted;
KW Kinase {ECO:0000313|EMBL:AEE15614.1}; Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000006546};
KW Transferase {ECO:0000313|EMBL:AEE15614.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 6..26
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 327..349
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 368..585
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
SQ SEQUENCE 586 AA; 64761 MW; 2B358CAD3977BA0D CRC64;
MKHSKTIVLV ALPATLILAV VVLFIMQIRF TLGQYRAELG YLTDEVTRNT TQTAFMIEDE
LLLLPVLAKM SGKTDSQDIS YEQVASNVSN AVKFWNKHAI VSELFSAIYL YAKNSLTESG
AATLQLWDGT GFAGAPPTQT RIITDMLDSV LQSKPEIADL WYISSPDIGE LIVSPITTEE
SDYVLISQID STVLSSKLIP ILTAKFFTGD SSYRIRVYDE TTGNLIYTNE KSYNPAHFTD
PDFSYRLFGS DRQKNGAFNR INPSWDLPIE LFSLKQENEI AGLRSHMRTK AAFNDDFSSG
IKPFPYNLTL EVVHKDGSVL SAAKKAAALN MTLSFIAFII LTAGIGILLR NMAKAQNLAD
RQQEFIASVT HELKTPLTVI SSSAQNMADG IITDAEKIRK YGKMICTESE KLRNSIEYFL
LYAKMNTAAK LPCRECNIGT LLESVAALLA PAAREAQMRV ELSLPPQELS VGCDENAIRS
VFRNLAENAI KHAAAGRYLH IEASREQEFA VVRFTDRGGG VPRKERKRIF DAFQRGNAAV
ENQTEGSGIG LNLSRRIVAL HGGSLELESS SSHGSVFTVR LPLQRS
//
