ID   ALKN_PSEOL              Reviewed;         492 AA.
AC   Q9R9U8;
DT   23-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 66.
DE   RecName: Full=Putative methyl-accepting chemotaxis AlkN;
GN   Name=alkN;
OS   Pseudomonas oleovorans.
OG   Plasmid OCT.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas;
OC   Pseudomonas oleovorans/pseudoalcaligenes group.
OX   NCBI_TaxID=301;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PATHWAY.
RC   STRAIN=ATCC 29347 / CIP 105816 / NRRL B-14683 / TF4-1L;
RX   PubMed=11390693; DOI=10.1099/00221287-147-6-1621;
RA   Van Beilen J.B., Panke S., Lucchini S., Franchini A.G., Roethlisberger M.,
RA   Witholt B.;
RT   "Analysis of Pseudomonas putida alkane degradation gene clusters and
RT   flanking insertion sequences: evolution and regulation of the alk-genes.";
RL   Microbiology 147:1621-1630(2001).
CC   -!- FUNCTION: Chemotactic-signal transducers respond to changes in the
CC       concentration of attractants and repellents in the environment,
CC       transduce a signal from the outside to the inside of the cell, and
CC       facilitate sensory adaptation through the variation of the level of
CC       methylation. {ECO:0000250}.
CC   -!- PATHWAY: Hydrocarbon metabolism; alkane degradation.
CC       {ECO:0000269|PubMed:11390693}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC       protein {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the methyl-accepting chemotaxis (MCP) protein
CC       family. {ECO:0000305}.
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DR   EMBL; AJ245436; CAB54058.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q9R9U8; -.
DR   SMR; Q9R9U8; -.
DR   PRIDE; Q9R9U8; -.
DR   UniPathway; UPA00191; -.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0004888; F:transmembrane signaling receptor activity; IEA:InterPro.
DR   GO; GO:0043448; P:alkane catabolic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0006935; P:chemotaxis; IEA:InterPro.
DR   GO; GO:0007165; P:signal transduction; IEA:UniProtKB-KW.
DR   InterPro; IPR004090; Chemotax_Me-accpt_rcpt.
DR   InterPro; IPR003660; HAMP_dom.
DR   InterPro; IPR004089; MCPsignal_dom.
DR   Pfam; PF00015; MCPsignal; 1.
DR   PRINTS; PR00260; CHEMTRNSDUCR.
DR   SMART; SM00283; MA; 1.
DR   PROSITE; PS50111; CHEMOTAXIS_TRANSDUC_2; 1.
DR   PROSITE; PS50885; HAMP; 1.
PE   3: Inferred from homology;
KW   Membrane; Plasmid; Transducer; Transmembrane; Transmembrane helix.
FT   CHAIN           1..492
FT                   /note="Putative methyl-accepting chemotaxis AlkN"
FT                   /id="PRO_0000392222"
FT   TRANSMEM        9..29
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        159..179
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          180..231
FT                   /note="HAMP"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00102"
FT   DOMAIN          236..472
FT                   /note="Methyl-accepting transducer"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00284"
SQ   SEQUENCE   492 AA;  53878 MW;  C74A436BAA6C6CEF CRC64;
     MNCSLRCRFF LILVMAGFSF FVALFGMRLM HKMAEFAYFE REHVVALSKV YYELHKKEIN
     ISFIVGQVQR ARRQTTAVNS LWKGDKALLR LLGKGLILEL SEASEIKLGL LERYASSIYK
     DGLNPGHIEE MKRLVSWPYT NSNRFGIEIA DISKRVKAYV YFLVVSINCL FFVVIFLLMK
     KTRSSIDEIV HVMNDMSRGD LTYRTIPSND EVGKMQSSII AMGAGVSALI ESIKHIQGDL
     FNSAGEALNI SQSTSNDICD QAGKIDEFVS ALSQISFAIT ETSNAANKSS ALSSEGRQLA
     VHGQKAIETA VSSINALSQR VNDSHVAIKC IEADIAKIGK IIEIIDQITD QTNLLALNAA
     IEAAHAGEAG KGFAVVADEV RSLAQRTNNS TYEIQAMIAS LNKGIFFALG VMGDCVVESK
     NSVNAASEAS RSIEKIVDSV SQVMLQIAQV ATASEEQSAV VKDMLDNANI IREIAAGVEL
     GSRRISEVNT HR