ID F4LPE6_TREBD Unreviewed; 337 AA.
AC F4LPE6;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 27-MAR-2024, entry version 47.
DE SubName: Full=Cache domain protein {ECO:0000313|EMBL:AEE15957.1};
GN OrderedLocusNames=Trebr_0514 {ECO:0000313|EMBL:AEE15957.1};
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:AEE15957.1, 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 -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP002696; AEE15957.1; -; Genomic_DNA.
DR RefSeq; WP_013757676.1; NC_015500.1.
DR AlphaFoldDB; F4LPE6; -.
DR STRING; 906968.Trebr_0514; -.
DR KEGG; tbe:Trebr_0514; -.
DR eggNOG; COG0840; Bacteria.
DR eggNOG; COG4191; Bacteria.
DR HOGENOM; CLU_047366_0_0_12; -.
DR Proteomes; UP000006546; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR GO; GO:0004888; F:transmembrane signaling receptor activity; IEA:InterPro.
DR GO; GO:0006935; P:chemotaxis; IEA:UniProtKB-KW.
DR GO; GO:0007165; P:signal transduction; IEA:UniProtKB-KW.
DR CDD; cd12914; PDC1_DGC_like; 1.
DR CDD; cd18774; PDC2_HK_sensor; 1.
DR Gene3D; 6.10.250.3200; -; 1.
DR Gene3D; 3.30.450.20; PAS domain; 2.
DR InterPro; IPR004090; Chemotax_Me-accpt_rcpt.
DR InterPro; IPR033479; dCache_1.
DR InterPro; IPR004089; MCPsignal_dom.
DR InterPro; IPR029151; Sensor-like_sf.
DR PANTHER; PTHR32089:SF92; LYSOZYME-LIKE PROTEIN-RELATED; 1.
DR PANTHER; PTHR32089; METHYL-ACCEPTING CHEMOTAXIS PROTEIN MCPB; 1.
DR Pfam; PF02743; dCache_1; 1.
DR Pfam; PF00015; MCPsignal; 1.
DR PRINTS; PR00260; CHEMTRNSDUCR.
DR SUPFAM; SSF58104; Methyl-accepting chemotaxis protein (MCP) signaling domain; 1.
DR SUPFAM; SSF103190; Sensory domain-like; 1.
DR PROSITE; PS50111; CHEMOTAXIS_TRANSDUC_2; 1.
PE 4: Predicted;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Chemotaxis {ECO:0000256|ARBA:ARBA00022500};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Reference proteome {ECO:0000313|Proteomes:UP000006546};
KW Transducer {ECO:0000256|ARBA:ARBA00023224, ECO:0000256|PROSITE-
KW ProRule:PRU00284}; Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT DOMAIN 1..90
FT /note="Methyl-accepting transducer"
FT /evidence="ECO:0000259|PROSITE:PS50111"
SQ SEQUENCE 337 AA; 37234 MW; DFD5714E86CB93C1 CRC64;
MALKTSNKKT EMSALFQTLI QNYGSLRAAL DTIYQLSQNI RLLSFNSSVE AARAGQAGRG
FRIIAGEIKK FSEKSDESNK LCGDVVNTIE GGMQQLIGVR TADMAFDLID KIDRNLFERN
CDVQAWATFG KIISALESPS AASLQSAREI LSNLVKIYEV YLDIVLCDLS GKVVCTGVTS
VLEGTDVSER EWFRRTVESG KVYVTDMYHS ATLNAQTVAY SCPVCSLSGQ LLGVISTRFN
WKFIYDIVDK AMIGRDGEIY VVNKQGTVIA SKNKGDVLNK SLSALPAMTR LQNGTDYGYD
IDAQKDGKLA VFGFARTQGY NAYRGKDWSV IVREIYQ
//