ID A0A418XJ49_9PSED Unreviewed; 682 AA.
AC A0A418XJ49;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 13.
DE SubName: Full=Chemotaxis protein {ECO:0000313|EMBL:RJG12455.1};
GN ORFNames=D3879_03970 {ECO:0000313|EMBL:RJG12455.1};
OS Pseudomonas cavernicola.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=2320866 {ECO:0000313|EMBL:RJG12455.1, ECO:0000313|Proteomes:UP000284021};
RN [1] {ECO:0000313|EMBL:RJG12455.1, ECO:0000313|Proteomes:UP000284021}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K1S02-6 {ECO:0000313|EMBL:RJG12455.1,
RC ECO:0000313|Proteomes:UP000284021};
RA Zhu H.;
RL Submitted (SEP-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:RJG12455.1}.
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DR EMBL; QYUR01000002; RJG12455.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A418XJ49; -.
DR OrthoDB; 9177152at2; -.
DR Proteomes; UP000284021; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004888; F:transmembrane signaling receptor activity; IEA:InterPro.
DR GO; GO:0006935; P:chemotaxis; IEA:InterPro.
DR GO; GO:0007165; P:signal transduction; IEA:UniProtKB-KW.
DR CDD; cd11386; MCP_signal; 1.
DR Gene3D; 1.10.287.950; Methyl-accepting chemotaxis protein; 1.
DR InterPro; IPR004090; Chemotax_Me-accpt_rcpt.
DR InterPro; IPR003660; HAMP_dom.
DR InterPro; IPR004089; MCPsignal_dom.
DR InterPro; IPR029095; NarX-like_N.
DR PANTHER; PTHR32089; METHYL-ACCEPTING CHEMOTAXIS PROTEIN MCPB; 1.
DR PANTHER; PTHR32089:SF119; METHYL-ACCEPTING CHEMOTAXIS PROTEIN TLPQ; 1.
DR Pfam; PF00015; MCPsignal; 1.
DR Pfam; PF13675; PilJ; 1.
DR PRINTS; PR00260; CHEMTRNSDUCR.
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|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 20..40
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 311..332
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 347..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 682 AA; 72366 MW; 6EDB63C9195D60D0 CRC64;
MKKLNAGNLL AGMRSSTLIA GLFIVLIVSI VLLFANFAYI NTQSNYDKEY ISHSGELRVL
SQRIAKNATE AAAGKVEAFA LLKDARNDFE KRWGFLVNGD ESTGLPSAPE AVQTEMSAVQ
QDWDSLRKNS DAILASEQTV LSLHQVAATL AETIPQLQVE YEEVVDILLE SGAPAAQVSV
AQRQSLLAER ILGSVNKVLA GDEDSVQAAD MFGRDASLFG RVLSAMLEGN AAMKIAKVTD
QEALERLAEI SELFEFVSGS VDEILETSPE LFQVRESASS IFSVSQTLLD KASQLASGFE
SLAGGRYLNT VVGYVLGLLA LASIILIGLV MVQSTRSRLA ETAEKNERNQ AAILRLLDEI
ADLADGDLTV AATVTEDFTG AIADSINYSI DQLRDLVATI NLTAVQVAAA AQETQATAMH
LAEASEHQAQ EIAGASAAIN EMAVSIDQVS ANASESSAVA ERSVAIANKG NEVVHNTITG
MDNIREQIQD TSKRIKRLGE SSQEIGDIVS LINDIADQTN ILALNAAIQA SMAGDAGRGF
AVVADEVQRL AERSSAATKQ IEALVKTIQT DTNEAVISME QTTSEVVRGA RLAQDAGVSL
EEIEKVSKTL AALIQNISNA ARQQASSAGH ISNTMNVIQE ITSQTSSGTT ATAKSIGNLA
KMASEMRRSV SGFTLPEATD QA
//
