ID A0A419T848_9FIRM Unreviewed; 663 AA.
AC A0A419T848;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 13-SEP-2023, entry version 17.
DE RecName: Full=Chemotaxis protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=BET01_14225 {ECO:0000313|EMBL:RKD33730.1};
OS Lacrimispora algidixylanolytica.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC Lacrimispora.
OX NCBI_TaxID=94868 {ECO:0000313|EMBL:RKD33730.1, ECO:0000313|Proteomes:UP000284277};
RN [1] {ECO:0000313|EMBL:RKD33730.1, ECO:0000313|Proteomes:UP000284277}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SPL73 {ECO:0000313|EMBL:RKD33730.1,
RC ECO:0000313|Proteomes:UP000284277};
RA Poppleton D.I., Gribaldo S.;
RT "A new outlook on sporulation: Clostridium algidixylanolyticum.";
RL Submitted (AUG-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 -!- 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:RKD33730.1}.
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DR EMBL; MCIA01000006; RKD33730.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A419T848; -.
DR Proteomes; UP000284277; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma 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 CDD; cd12913; PDC1_MCP_like; 1.
DR CDD; cd12912; PDC2_MCP_like; 1.
DR Gene3D; 6.10.340.10; -; 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; PTHR43531:SF11; METHYL-ACCEPTING CHEMOTAXIS PROTEIN 3; 1.
DR PANTHER; PTHR43531; PROTEIN ICFG; 1.
DR Pfam; PF02743; dCache_1; 1.
DR Pfam; PF00672; HAMP; 1.
DR Pfam; PF00015; MCPsignal; 1.
DR SMART; SM00304; HAMP; 2.
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 Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000284277};
KW Transducer {ECO:0000256|PROSITE-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 6..27
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 289..311
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 313..365
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 418..647
FT /note="Methyl-accepting transducer"
FT /evidence="ECO:0000259|PROSITE:PS50111"
SQ SEQUENCE 663 AA; 71508 MW; 429AAEECD4CABE8C CRC64;
MAKILIYIGI PVVLSYCIVG LILLNLVRGN IEQLTEGNLE AKSQTASVEM EQFFDRFRNS
ADQLSKSVQL QKFFADLKPG AKISEGQDFK EVVQSLKNIS DTDKDNILSI WVSDVDSSQL
AQSNGFVSDS SYQISERPWY QMLLKEQKTV MTEPYEDFTS KAQIVSIIAP VYSENGGQMV
GAVGIDFSLD GLKKTIGDYH LGTTGFYIVT SADGQIIYHP KEEMINKNVS EQDMSDGIKQ
AFLKSIEGKI QYTSHGVSVH GYVSRIGDTG WMVGTGLPLK EFYNEYNKIT TAMAFIFMVA
AALVVGMIFI VSKGIVAPLK TLTNAANLIA DGRLDISADV NSRDETGQLA HALNRTVVQL
NGYIGYIREI TTVLETMAGG DIRINLNQDY AGEFKPIKEA LLQISDSLNK TLTSIRITAD
QVNTGAEQVS SAAQALASGS TEQAATVEEL SASIISISTQ AEQNAENVRK ASDYVRQAGE
GLEESNHHME RLNAAMDEIS DSSAKISSIT KVIEDIAFQT NILALNAAVE AARAGEAGKG
FAVVADEVRN LAAKSAEAAK QTSELIGLST VTVAEGEKMA SETSKTLKDV ALKSQLVVEV
IRDINKASAE QAVSIGEINQ GLSQVSAVVQ TNAATAEESS ASSEELAAQA QLLKNEVSKF
TLY
//
