ID C4ZC11_AGARV Unreviewed; 570 AA.
AC C4ZC11;
DT 28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 28-JUL-2009, sequence version 1.
DT 27-MAR-2024, entry version 70.
DE SubName: Full=Putative methyl-accepting chemotaxis protein (MCP) {ECO:0000313|EMBL:ACR74301.1};
GN OrderedLocusNames=EUBREC_0510 {ECO:0000313|EMBL:ACR74301.1};
OS Agathobacter rectalis (strain ATCC 33656 / DSM 3377 / JCM 17463 / KCTC 5835
OS / VPI 0990) (Eubacterium rectale).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC Agathobacter.
OX NCBI_TaxID=515619 {ECO:0000313|EMBL:ACR74301.1, ECO:0000313|Proteomes:UP000001477};
RN [1] {ECO:0000313|EMBL:ACR74301.1, ECO:0000313|Proteomes:UP000001477}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33656 / DSM 3377 / JCM 17463 / KCTC 5835 / LMG 30912 / VPI
RC 0990 {ECO:0000313|Proteomes:UP000001477};
RX PubMed=19321416; DOI=10.1073/pnas.0901529106;
RA Mahowald M.A., Rey F.E., Seedorf H., Turnbaugh P.J., Fulton R.S.,
RA Wollam A., Shah N., Wang C., Magrini V., Wilson R.K., Cantarel B.L.,
RA Coutinho P.M., Henrissat B., Crock L.W., Russell A., Verberkmoes N.C.,
RA Hettich R.L., Gordon J.I.;
RT "Characterizing a model human gut microbiota composed of members of its two
RT dominant bacterial phyla.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:5859-5864(2009).
CC -!- SIMILARITY: Belongs to the methyl-accepting chemotaxis (MCP) protein
CC family. {ECO:0000256|ARBA:ARBA00029447}.
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DR EMBL; CP001107; ACR74301.1; -; Genomic_DNA.
DR RefSeq; WP_012741418.1; NC_012781.1.
DR AlphaFoldDB; C4ZC11; -.
DR STRING; 515619.EUBREC_0510; -.
DR PaxDb; 515619-EUBREC_0510; -.
DR KEGG; ere:EUBREC_0510; -.
DR HOGENOM; CLU_000445_107_16_9; -.
DR Proteomes; UP000001477; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0007165; P:signal transduction; IEA:UniProtKB-KW.
DR CDD; cd06225; HAMP; 1.
DR CDD; cd11386; MCP_signal; 1.
DR Gene3D; 6.10.340.10; -; 1.
DR Gene3D; 1.10.287.950; Methyl-accepting chemotaxis protein; 1.
DR InterPro; IPR003660; HAMP_dom.
DR InterPro; IPR024478; HlyB_4HB_MCP.
DR InterPro; IPR004089; MCPsignal_dom.
DR PANTHER; PTHR43531:SF11; METHYL-ACCEPTING CHEMOTAXIS PROTEIN 3; 1.
DR PANTHER; PTHR43531; PROTEIN ICFG; 1.
DR Pfam; PF12729; 4HB_MCP_1; 1.
DR Pfam; PF00672; HAMP; 1.
DR Pfam; PF00015; MCPsignal; 1.
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 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 23..48
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 189..209
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 219..271
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 321..550
FT /note="Methyl-accepting transducer"
FT /evidence="ECO:0000259|PROSITE:PS50111"
SQ SEQUENCE 570 AA; 62449 MW; A349D356AF71380F CRC64;
MSSKKDAMKK KLENMHLGER INYGYRMVIT MMLISGLLSI AVIGVLFFNM LNYVNKVNAA
DQAVKTCRIN VNAAARNVRE MALNPDKSTY DDYEQGAKEK LEDVDVQLKT IKKSGIVPEN
QYNEYSKALS DWANIGYSIM DKIKAGQKDE AVDQIINECT PKLNKTVELA KEINKLTDER
SHQAVVRTYV CAAVGLIVII ICLICAWQLT KRTGKIVLDT ILEPLHAIEE VAKELTEGNL
HSTLDYRSED EIGRLAHSMR KSIRILGSYV DDIDRSMKLF ADGHFDAQPE VEWRGDFVGI
LHSFMEFEKS MAVTIKGIQN VSSEVSSAAE QVAASSNDLA DGATNQAAVV EELTATVEGV
SEQVEQNSKS AKEISGRVDE LGGAIWESNG KMQEMVTSMH EINEASKQID QIISTINEIA
SQTNLLALNA SIEAARAGEA GKGFAVVANQ VNMLADQSAQ AAKESAALIE TSVQAVEKGM
NIAEQTASQL EEVAENSKVI TKEVTNIADT LETQTSEIKQ INEGIEQIND VVQTNSATSQ
ECAAASQQMS SESENLSEMI AKFKISDIEE
//
