ID F5YNH8_TREPZ Unreviewed; 513 AA.
AC F5YNH8;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 27-JUL-2011, sequence version 1.
DT 27-MAR-2024, entry version 61.
DE SubName: Full=Putative histidine kinase internal region {ECO:0000313|EMBL:AEF84400.1};
GN OrderedLocusNames=TREPR_3005 {ECO:0000313|EMBL:AEF84400.1};
OS Treponema primitia (strain ATCC BAA-887 / DSM 12427 / ZAS-2).
OC Bacteria; Spirochaetota; Spirochaetia; Spirochaetales; Treponemataceae;
OC Treponema.
OX NCBI_TaxID=545694 {ECO:0000313|EMBL:AEF84400.1, ECO:0000313|Proteomes:UP000009223};
RN [1] {ECO:0000313|Proteomes:UP000009223}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-887 / DSM 12427 / ZAS-2
RC {ECO:0000313|Proteomes:UP000009223};
RA Tetu S.G., Matson E., Ren Q., Seshadri R., Elbourne L., Hassan K.A.,
RA Durkin A., Radune D., Mohamoud Y., Shay R., Jin S., Zhang X., Lucey K.,
RA Ballor N.R., Ottesen E., Rosenthal R., Allen A., Leadbetter J.R.,
RA Paulsen I.T.;
RT "Complete sequence of Treponema primitia strain ZAS-2.";
RL Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:AEF84400.1, ECO:0000313|Proteomes:UP000009223}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-887 / DSM 12427 / ZAS-2
RC {ECO:0000313|Proteomes:UP000009223};
RX PubMed=21326336; DOI=10.1038/ismej.2011.3;
RA Rosenthal A.Z., Matson E.G., Eldar A., Leadbetter J.R.;
RT "RNA-seq reveals cooperative metabolic interactions between two termite-gut
RT spirochete species in co-culture.";
RL ISME J. 5:1133-1142(2011).
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DR EMBL; CP001843; AEF84400.1; -; Genomic_DNA.
DR AlphaFoldDB; F5YNH8; -.
DR STRING; 545694.TREPR_3005; -.
DR KEGG; tpi:TREPR_3005; -.
DR eggNOG; COG2972; Bacteria.
DR HOGENOM; CLU_020473_5_1_12; -.
DR Proteomes; UP000009223; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd06225; HAMP; 1.
DR Gene3D; 6.10.340.10; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR InterPro; IPR003660; HAMP_dom.
DR InterPro; IPR036890; HATPase_C_sf.
DR InterPro; IPR010559; Sig_transdc_His_kin_internal.
DR PANTHER; PTHR34220; SENSOR HISTIDINE KINASE YPDA; 1.
DR PANTHER; PTHR34220:SF7; SENSOR HISTIDINE KINASE YPDA; 1.
DR Pfam; PF00672; HAMP; 1.
DR Pfam; PF06580; His_kinase; 1.
DR SMART; SM00304; HAMP; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF158472; HAMP domain-like; 1.
DR PROSITE; PS50885; HAMP; 1.
PE 4: Predicted;
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:AEF84400.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000009223};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..36
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 184..205
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 206..259
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
SQ SEQUENCE 513 AA; 58944 MW; D4589468428E0028 CRC64;
MKSPLGRIRG SIRLQMLFSG VGVFLILVLS TAYILFSSIR LQAVSARSFE KERFIKSIQE
GLEAFQEPLL NYLSTRSSNA LSRILIDTQA LRWKLPTYMP ITVNQSELKE RELYSLIHSY
LNLADQAMEE KRGRNVSAYT RIYDEMEGLL GYINNEIDHI STERFRSQLD AYGIFIADAW
AVQFWNFLFI IFISIFAILM LFSSIRRITS PLVRLSAMAV EISAGNFGVN DIEPSSVEEM
DQLVRAFNRM KHDISQYVEA IRRQENIRQE YMQERLRNMN MEGLVRHMEI YALQAQMNPH
FLFNTLNTGM QLAIVEGADR TGEYMEYLAR LFRHIIRNKE IIVPLRHEIE GMNYYFYLLR
VRFPKSLDLA MDCDEALLDR YKVPVSILQP LVENCVVHAF KNVPAYPEES SARASHIRVS
AALEGERLVL QVVDNGSGMT GETREKLLHP QSIAQSSLSR VMGLENVIQR LYFFYPDDPE
VVDIKSGEGG EGTAIIIRIN TLREPSYPGG SRV
//
