ID A0A369B489_9FIRM Unreviewed; 682 AA.
AC A0A369B489;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE SubName: Full=Methyl-accepting chemotaxis protein {ECO:0000313|EMBL:RCX16271.1};
GN ORFNames=DFR58_11114 {ECO:0000313|EMBL:RCX16271.1};
OS Anaerobacterium chartisolvens.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae;
OC Anaerobacterium.
OX NCBI_TaxID=1297424 {ECO:0000313|EMBL:RCX16271.1, ECO:0000313|Proteomes:UP000253034};
RN [1] {ECO:0000313|EMBL:RCX16271.1, ECO:0000313|Proteomes:UP000253034}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 27016 {ECO:0000313|EMBL:RCX16271.1,
RC ECO:0000313|Proteomes:UP000253034};
RA Goeker M.;
RT "Genomic Encyclopedia of Type Strains, Phase IV (KMG-IV): sequencing the
RT most valuable type-strain genomes for metagenomic binning, comparative
RT biology and taxonomic classification.";
RL Submitted (JUL-2018) 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 -!- 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:RCX16271.1}.
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DR EMBL; QPJT01000011; RCX16271.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A369B489; -.
DR OrthoDB; 1062at2; -.
DR Proteomes; UP000253034; 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; cd12914; PDC1_DGC_like; 1.
DR CDD; cd12912; PDC2_MCP_like; 1.
DR Gene3D; 1.10.287.950; Methyl-accepting chemotaxis protein; 1.
DR Gene3D; 3.30.450.20; PAS domain; 1.
DR InterPro; IPR033479; dCache_1.
DR InterPro; IPR003660; HAMP_dom.
DR InterPro; IPR004089; MCPsignal_dom.
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 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 Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Chemotaxis {ECO:0000256|ARBA:ARBA00022500};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000253034};
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 301..320
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 321..376
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 395..666
FT /note="Methyl-accepting transducer"
FT /evidence="ECO:0000259|PROSITE:PS50111"
SQ SEQUENCE 682 AA; 73271 MW; 6A6569F2D28F4296 CRC64;
MKSLKTKIIM LMSCILIIVC AGLGSVSYYN ASAVVKKNTQ DMLQRLAVEA SRTVEARISS
QFNSLEILAE SNILDSIIKD DADRIQSNLV LAEEVKRMGH IKMGVADTAG NAVYSDGSRA
DIGEQDYFKK AAGGEHAMSS PFIDAESNAV VMMYAVPITV NGETVGVLAA VRDGYELSNF
AKEIVIGKTG KTFIVDSAAR TIGHADIELQ KQLIQSGSKK ADAVSSASVE AGEAQSNAGF
KNYDTLQKRM ISGETGFGEY EYRGAGMYLG FAPVKDLNWS VAIQANKEEM LSSLSGLRIT
YLWISLIFLI AGIVAVYLFS TRLTRHLSSM KKYASLLQGF DLSQDIADNL IKQKDEVGQL
AGAFSIFVIK IRALVHGIKA TAAKTTESAG QISAAAKATG ESAEQIAVSS GEVAKGTSKQ
SEFVDTVMEL INKNKDEVGK GFEMVDQALN NAQISTKIAE EGRNSIFASM EQLSDISKTV
ELAAGSMQNL SVRSKEIGKI VGVITGIASQ TDLLALNASI EAARAGEAGR GFSVVADEIR
NLAEGSGEAA RSIKQLINDI RRETELTVKT MEGSMDKVNT QVDQIKLGGE ALEKIVDMVV
RTENGVTQIH TSFKTIQTLS DDIVNAVFEI SAIIQEASAH SQQVAAATEE QTAASEEMSA
RAEELLLMAT RLKEELYVFK TE
//
