ID A0A1H4FQU3_9FIRM Unreviewed; 642 AA.
AC A0A1H4FQU3;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Methyl-accepting chemotaxis protein {ECO:0000313|EMBL:SEA99427.1};
GN ORFNames=SAMN02910384_02990 {ECO:0000313|EMBL:SEA99427.1};
OS Pseudobutyrivibrio sp. ACV-2.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC Pseudobutyrivibrio.
OX NCBI_TaxID=1520801 {ECO:0000313|EMBL:SEA99427.1, ECO:0000313|Proteomes:UP000199179};
RN [1] {ECO:0000313|Proteomes:UP000199179}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ACV-2 {ECO:0000313|Proteomes:UP000199179};
RA Varghese N., Submissions S.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the methyl-accepting chemotaxis (MCP) protein
CC family. {ECO:0000256|ARBA:ARBA00029447}.
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; FNQZ01000021; SEA99427.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H4FQU3; -.
DR STRING; 1520801.SAMN02910384_02990; -.
DR Proteomes; UP000199179; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR GO; GO:0006935; P:chemotaxis; IEA:UniProtKB-KW.
DR GO; GO:0007165; P:signal transduction; IEA:UniProtKB-KW.
DR CDD; cd06225; HAMP; 1.
DR Gene3D; 1.10.287.950; Methyl-accepting chemotaxis protein; 1.
DR Gene3D; 3.30.450.20; PAS domain; 2.
DR InterPro; IPR033479; dCache_1.
DR InterPro; IPR003660; HAMP_dom.
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; 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 SUPFAM; SSF103190; Sensory domain-like; 1.
DR PROSITE; PS50111; CHEMOTAXIS_TRANSDUC_2; 1.
DR PROSITE; PS50885; HAMP; 1.
PE 3: Inferred from homology;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Chemotaxis {ECO:0000256|ARBA:ARBA00022500};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Transducer {ECO:0000256|ARBA:ARBA00023224, ECO:0000256|PROSITE-
KW ProRule:PRU00284};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 250..273
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 275..327
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 346..596
FT /note="Methyl-accepting transducer"
FT /evidence="ECO:0000259|PROSITE:PS50111"
SQ SEQUENCE 642 AA; 69795 MW; ADDEBE57C6D39F09 CRC64;
MMKKLINSSL NNEVVVDAGQ INKALNSIFY YLNGIADSTE KLHFEDNAEI IDYLSQTVGR
YDLIPTGAYI GTNTDEFLDP SGWVPGEDYM VTEKKWYQQG IGYDNTWFYY YDQPYFDAAT
GDLCATVILH IHLKDGREGV FAADLILTAL QSQLNEVTLY KTGGCIMVTA EGQILSYRDT
TLCGTNIADN SSDQFWKAVG ENLSAEDNVV STVKTQGASY YMVSSTVSGT DWKVIVYAKR
TEVLEELIRL VYVLIAATII VVLLVVALVL RVLSNMIKKP VTMLTENIEK IASGDFTVEI
TSTGNDEIAF MNSAMGKFIN GMRDSLSEIK SVSTKLIGDA QNSKDTAENL KLAANEQSAS
MSQIRDNIDD MAEAVNEVAE NATALAHTIS DVTTEEEQIE DIMNQLVKKA DVGQNDMKSV
AEGMDHIVSS MKDMSEAVQS VDDAAQQITQ IVDMINSISS QTNLLSLNAS IEAARAGEAG
KGFAVVATEI GALANNSAEA TNQIVDIIRE MSDRVKDLSE KSETNSQLID ESSGSINAAA
ETFLQITTEL NNASSTLKDM AEQMRKVNDV ATNMASVSEQ QSASTQMIAS NVERVTMASQ
EVADSSDQVA IAATNVSNAV DTINNNLVKF TIEASNEIKN QL
//
