ID A0A2A4WE17_9GAMM Unreviewed; 677 AA.
AC A0A2A4WE17;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=Methyl-accepting chemotaxis protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=COB33_11025 {ECO:0000313|EMBL:PCI67977.1};
OS Thiotrichaceae bacterium.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Thiotrichales;
OC Thiotrichaceae.
OX NCBI_TaxID=2030882 {ECO:0000313|EMBL:PCI67977.1, ECO:0000313|Proteomes:UP000217494};
RN [1] {ECO:0000313|Proteomes:UP000217494}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Tully B.J., Wheat C.G., Glazer B.T., Huber J.A.;
RT "A dynamic microbial community with high functional redundancy inhabits the
RT cold, oxic subseafloor aquifer.";
RL Submitted (AUG-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the methyl-accepting chemotaxis (MCP) protein
CC family. {ECO:0000256|ARBA:ARBA00029447}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PCI67977.1}.
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DR EMBL; NVTY01000030; PCI67977.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2A4WE17; -.
DR Proteomes; UP000217494; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0006935; P:chemotaxis; IEA:UniProt.
DR GO; GO:0007165; P:signal transduction; IEA:UniProtKB-KW.
DR CDD; cd06225; HAMP; 1.
DR Gene3D; 3.30.450.290; -; 1.
DR Gene3D; 1.10.8.500; HAMP domain in histidine kinase; 1.
DR Gene3D; 1.10.287.950; Methyl-accepting chemotaxis protein; 1.
DR InterPro; IPR003660; HAMP_dom.
DR InterPro; IPR004089; MCPsignal_dom.
DR PANTHER; PTHR32089:SF112; HEME-BASED AEROTACTIC TRANSDUCER HEMAT; 1.
DR PANTHER; PTHR32089; METHYL-ACCEPTING CHEMOTAXIS PROTEIN MCPB; 1.
DR Pfam; PF00672; HAMP; 2.
DR Pfam; PF00015; MCPsignal; 1.
DR SMART; SM00304; HAMP; 3.
DR SMART; SM00283; MA; 1.
DR SUPFAM; SSF158472; HAMP domain-like; 1.
DR SUPFAM; SSF58104; Methyl-accepting chemotaxis protein (MCP) signaling domain; 1.
DR PROSITE; PS50111; CHEMOTAXIS_TRANSDUC_2; 1.
DR PROSITE; PS50885; HAMP; 3.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Transducer {ECO:0000256|ARBA:ARBA00023224, ECO:0000256|PROSITE-
KW ProRule:PRU00284}; Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 21..40
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 201..219
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 221..273
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 293..339
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 363..398
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 403..639
FT /note="Methyl-accepting transducer"
FT /evidence="ECO:0000259|PROSITE:PS50111"
SQ SEQUENCE 677 AA; 72930 MW; 9834279E1F503DB4 CRC64;
MASQERGSLF GHLSVRMKIN LTVAIIFVFV ISMVTGYTVY IEKQRAQDDA EERTQDLATF
YFDSLNTMML TNTMDQRSIL RDKVLKRNNV VDARVIRGEP VNQQYGPGFP EEAPVDDWDR
RALLGEDIME LQEGKDFDKG VEGRVLTVLT PFRATSGENP GDVNCLACHN VPENSVNGAI
RVSYSLQNID ETIAKDVRTQ IIANVVLLVV GLLLANFLLG KWLSAPLKRV MDTVNQRAEG
DLTVRISISS LDEIGKLGMA FNTMADNVDG ANQQQQIQAQ REHDAAEVLK EKVNVLLDVV
NRAAEGDLTG VVTFSGDDAI GSLGFGLQSM VHNLSELMEE RRIAMEDLEE KVGKMQIVVQ
CAAAGDLTGE IDVSGDDAVG RMAQGIQAMI NSLNGLVSQV QQSGIQVTSS STEIAASAKQ
QEATVAEQAA TVNEIVATAT EISATGKELV NTMDEVAGVA SGTAEAAASG HTGLIRMEET
MHSVVDASNA IASKLEVLSE KAGNINSVVT TITKVADQTN LLSLNAAIEA EKAGEYGVGF
AVVATEIRRL ADQTAVATLD IEQMVQEMQS AVSAGVMSVE KFSKEVKNSV DDVREVGAQL
AQIIDQVQTL TPRFEIVHEG MHMQSEGAEQ IKQAMIQLSE SAQQTVESLR QSNSAIDRLN
DAAHGLQGGV SQFKIDS
//
