ID   ALKN_ALCBS              Reviewed;         675 AA.
AC   Q0VTI9;
DT   23-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 1.
DT   25-MAY-2022, entry version 79.
DE   RecName: Full=Putative methyl-accepting chemotaxis AlkN;
GN   OrderedLocusNames=ABO_0106;
OS   Alcanivorax borkumensis (strain ATCC 700651 / DSM 11573 / NCIMB 13689 /
OS   SK2).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Oceanospirillales;
OC   Alcanivoracaceae; Alcanivorax.
OX   NCBI_TaxID=393595;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700651 / DSM 11573 / NCIMB 13689 / SK2;
RX   PubMed=16878126; DOI=10.1038/nbt1232;
RA   Schneiker S., Martins dos Santos V.A.P., Bartels D., Bekel T., Brecht M.,
RA   Buhrmester J., Chernikova T.N., Denaro R., Ferrer M., Gertler C.,
RA   Goesmann A., Golyshina O.V., Kaminski F., Khachane A.N., Lang S., Linke B.,
RA   McHardy A.C., Meyer F., Nechitaylo T., Puehler A., Regenhardt D., Rupp O.,
RA   Sabirova J.S., Selbitschka W., Yakimov M.M., Timmis K.N., Vorhoelter F.-J.,
RA   Weidner S., Kaiser O., Golyshin P.N.;
RT   "Genome sequence of the ubiquitous hydrocarbon-degrading marine bacterium
RT   Alcanivorax borkumensis.";
RL   Nat. Biotechnol. 24:997-1004(2006).
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   -!- 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; AM286690; CAL15554.1; -; Genomic_DNA.
DR   RefSeq; WP_011587404.1; NC_008260.1.
DR   AlphaFoldDB; Q0VTI9; -.
DR   SMR; Q0VTI9; -.
DR   STRING; 393595.ABO_0106; -.
DR   EnsemblBacteria; CAL15554; CAL15554; ABO_0106.
DR   KEGG; abo:ABO_0106; -.
DR   eggNOG; COG0840; Bacteria.
DR   HOGENOM; CLU_000445_107_27_6; -.
DR   OMA; NTIHGMD; -.
DR   OrthoDB; 477199at2; -.
DR   UniPathway; UPA00191; -.
DR   Proteomes; UP000008871; Chromosome.
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   InterPro; IPR029095; NarX-like_N.
DR   Pfam; PF00015; MCPsignal; 1.
DR   Pfam; PF13675; PilJ; 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; Reference proteome; Transducer; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..675
FT                   /note="Putative methyl-accepting chemotaxis AlkN"
FT                   /id="PRO_0000392221"
FT   TRANSMEM        24..44
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        303..323
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          343..394
FT                   /note="HAMP"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00102"
FT   DOMAIN          399..635
FT                   /note="Methyl-accepting transducer"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00284"
SQ   SEQUENCE   675 AA;  71939 MW;  6F2B26654CB33037 CRC64;
     MKFNSGALFE KLRGGAGEGN TLNIALYVGL AIFIVLALAN FLLSATTANK AQENITRASE
     MRVISQQIAK NALEAAAGNA DAFELLDKSQ KGFQSAWNAV KDEQVSDPEA MARLQTLWDE
     VNANADVILK GEDTVLDLHE VADTLAQTIP SLQAEYEGVV EILVTTDAAP EQIAFAQRQS
     WLAERIVRSI AKVLEGGDGA VIAADSFGRD ASLFGRIMNG MIEGDAAMGI DQVNDPDALD
     YLAEIADLFD EFVNQSVDEI LETAPELFQV RNAADTIFRR SQDLLEESTN LNNQFENTTS
     GLFPSVWLGG VSAGLAVLFF FIIMAQRNRQ AAKLKDELES ENQRNQAAIL RLLDELGDLA
     DGDLTVQATV TEDFTGAIAD SINYSIDQLR NLVQTINNSA VQVASAAQET QSTAMHLAEA
     SEHQAQEIAG ASAAVNEMAV SIDQVSANAA ESAAVAERAV AIANKGAEVV QATIHGMDTI
     REQIQETSKR IKRLGESSQE IGDIVSLIND IADQTNILAL NAAIQASMAG EAGRGFAVVA
     DEVQRLAERS AAATKQIETL VKTIQTDTNE AVISMEATTA EVVKGARLAQ DAGVALEEIE
     SVSKTLADLI QNISNAARQQ AASAGHISNT MNVIQEITSQ TSAGTTATAR SIGNLAEMAQ
     DMRNSVAGFR LPEHS