ID G0ELU7_BRAIP Unreviewed; 487 AA.
AC G0ELU7;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 46.
DE SubName: Full=Methyl-accepting chemotaxis protein McpB {ECO:0000313|EMBL:AEM22796.1};
GN OrderedLocusNames=Bint_2188 {ECO:0000313|EMBL:AEM22796.1};
OS Brachyspira intermedia (strain ATCC 51140 / PWS/A) (Serpulina intermedia).
OC Bacteria; Spirochaetota; Spirochaetia; Brachyspirales; Brachyspiraceae;
OC Brachyspira.
OX NCBI_TaxID=1045858 {ECO:0000313|EMBL:AEM22796.1, ECO:0000313|Proteomes:UP000008522};
RN [1] {ECO:0000313|EMBL:AEM22796.1, ECO:0000313|Proteomes:UP000008522}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51140 / PWS/A {ECO:0000313|Proteomes:UP000008522};
RX PubMed=21816042; DOI=10.1186/1471-2164-12-395;
RA Hafstrom T., Jansson D.S., Segerman B.;
RT "Complete genome sequence of Brachyspira intermedia reveals unique genomic
RT features in Brachyspira species and phage-mediated horizontal gene
RT transfer.";
RL BMC Genomics 12:395-395(2011).
CC -!- SIMILARITY: Belongs to the methyl-accepting chemotaxis (MCP) protein
CC family. {ECO:0000256|ARBA:ARBA00029447}.
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DR EMBL; CP002874; AEM22796.1; -; Genomic_DNA.
DR AlphaFoldDB; G0ELU7; -.
DR KEGG; bip:Bint_2188; -.
DR PATRIC; fig|1045858.4.peg.2192; -.
DR eggNOG; COG0840; Bacteria.
DR HOGENOM; CLU_000445_107_12_12; -.
DR Proteomes; UP000008522; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0004888; F:transmembrane signaling receptor activity; IEA:InterPro.
DR GO; GO:0006935; P:chemotaxis; IEA:InterPro.
DR GO; GO:0007165; P:signal transduction; IEA:UniProtKB-KW.
DR CDD; cd11386; MCP_signal; 1.
DR Gene3D; 1.10.287.950; Methyl-accepting chemotaxis protein; 1.
DR InterPro; IPR004090; Chemotax_Me-accpt_rcpt.
DR InterPro; IPR003660; HAMP_dom.
DR InterPro; IPR004089; MCPsignal_dom.
DR PANTHER; PTHR43531:SF14; METHYL-ACCEPTING CHEMOTAXIS PROTEIN I-RELATED; 1.
DR PANTHER; PTHR43531; PROTEIN ICFG; 1.
DR Pfam; PF00672; HAMP; 1.
DR Pfam; PF00015; MCPsignal; 1.
DR PRINTS; PR00260; CHEMTRNSDUCR.
DR SMART; SM00304; HAMP; 1.
DR SMART; SM00283; MA; 1.
DR SUPFAM; SSF58104; Methyl-accepting chemotaxis protein (MCP) signaling domain; 1.
DR PROSITE; PS50111; CHEMOTAXIS_TRANSDUC_2; 1.
DR PROSITE; PS50885; HAMP; 1.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils}; Membrane {ECO:0000256|SAM:Phobius};
KW Transducer {ECO:0000256|PROSITE-ProRule:PRU00284};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 161..181
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 183..238
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 243..472
FT /note="Methyl-accepting transducer"
FT /evidence="ECO:0000259|PROSITE:PS50111"
FT COILED 384..411
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 487 AA; 53465 MW; 73D17EBFE601E9B1 CRC64;
MATANQKYEQ AYNDCIGISG GTKPTPLNYD RGLYWSLYLG SGTKPYQDGQ TKSYADVMKE
LNFSQDMFDL LALSKSRSEE LVKLEVQAMD IIKSIPRNAD GTIPDEYKGR QLEAIELVNG
DEYERRVSEI MTPISQFFDK LESDNAIKLR AAAYEVRNDT ILFFIGLLLV GSSVVVFLAS
LGKTIGKNLR LCVELASEIS NGNLTAEIDE RLCKGNGEFA SLLKSFRDMI SHLREIISRV
LQSSKEISEA ATEIAQGNTD LSTRTEMQAS HLEETASSME QIASTIKSSA DNSVRGNQMM
QDSEKSVQEA GEIIEATTNN IELVFEASNK ITDITKIIEN IAFQTNILAL NAAVEAARAG
EQGKGFAVVA SEVRNLAQTS QSSVKDITSL IADANEKIKT ATETARKSKE IFMDIEQKIE
DTSRIMQDIS AMAVEQQAGV DQVNIAVSQM DQSTQQNAAL VEQATASSEG LMGQAKELVD
LMHFFKV
//
