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Database: UniProt
Entry: F0J6R4_ACIMA
LinkDB: F0J6R4_ACIMA
Original site: F0J6R4_ACIMA 
ID   F0J6R4_ACIMA            Unreviewed;       631 AA.
AC   F0J6R4;
DT   03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   03-MAY-2011, sequence version 1.
DT   27-MAR-2024, entry version 57.
DE   SubName: Full=Methyl-accepting chemotaxis protein {ECO:0000313|EMBL:BAJ82681.1};
GN   OrderedLocusNames=ACMV_33340 {ECO:0000313|EMBL:BAJ82681.1};
OS   Acidiphilium multivorum (strain DSM 11245 / JCM 8867 / NBRC 100883 / AIU
OS   301).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC   Acetobacteraceae; Acidiphilium.
OX   NCBI_TaxID=926570 {ECO:0000313|EMBL:BAJ82681.1, ECO:0000313|Proteomes:UP000007100};
RN   [1] {ECO:0000313|EMBL:BAJ82681.1, ECO:0000313|Proteomes:UP000007100}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 11245 / JCM 8867 / AIU301
RC   {ECO:0000313|Proteomes:UP000007100};
RA   Narita-Yamada S., Nakamura S., Ito N., Takarada H., Katano Y., Nakazawa H.,
RA   Hosoyama A., Yamada R., Fujita N.;
RT   "Whole genome sequence of Acidiphilium multivorum AIU301.";
RL   Submitted (DEC-2010) 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}.
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DR   EMBL; AP012035; BAJ82681.1; -; Genomic_DNA.
DR   RefSeq; WP_007423431.1; NZ_BANA01000060.1.
DR   AlphaFoldDB; F0J6R4; -.
DR   KEGG; amv:ACMV_33340; -.
DR   HOGENOM; CLU_000445_107_16_5; -.
DR   OrthoDB; 7260004at2; -.
DR   Proteomes; UP000007100; Chromosome.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
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; cd06225; HAMP; 1.
DR   CDD; cd11386; MCP_signal; 1.
DR   Gene3D; 1.10.8.500; HAMP domain in histidine kinase; 1.
DR   Gene3D; 1.10.287.950; Methyl-accepting chemotaxis protein; 1.
DR   Gene3D; 3.30.450.20; PAS domain; 1.
DR   InterPro; IPR004090; Chemotax_Me-accpt_rcpt.
DR   InterPro; IPR003660; HAMP_dom.
DR   InterPro; IPR004089; MCPsignal_dom.
DR   InterPro; IPR033480; sCache_2.
DR   PANTHER; PTHR43531:SF11; METHYL-ACCEPTING CHEMOTAXIS PROTEIN 3; 1.
DR   PANTHER; PTHR43531; PROTEIN ICFG; 1.
DR   Pfam; PF00672; HAMP; 1.
DR   Pfam; PF00015; MCPsignal; 1.
DR   Pfam; PF17200; sCache_2; 1.
DR   PRINTS; PR00260; CHEMTRNSDUCR.
DR   SMART; SM01049; Cache_2; 1.
DR   SMART; SM00304; HAMP; 2.
DR   SMART; SM00283; MA; 1.
DR   SUPFAM; SSF158472; HAMP domain-like; 1.
DR   SUPFAM; SSF58104; Methyl-accepting chemotaxis protein (MCP) signaling domain; 1.
DR   PROSITE; PS50111; CHEMOTAXIS_TRANSDUC_2; 1.
DR   PROSITE; PS50885; HAMP; 2.
PE   3: Inferred from homology;
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
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        12..36
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        187..208
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          210..263
FT                   /note="HAMP"
FT                   /evidence="ECO:0000259|PROSITE:PS50885"
FT   DOMAIN          291..343
FT                   /note="HAMP"
FT                   /evidence="ECO:0000259|PROSITE:PS50885"
FT   DOMAIN          348..577
FT                   /note="Methyl-accepting transducer"
FT                   /evidence="ECO:0000259|PROSITE:PS50111"
FT   REGION          596..631
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        602..616
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   631 AA;  67085 MW;  14E5794C72FFA557 CRC64;
     MLHKLSIRHQ FAAIGLFGIT MTIAALVISL LGAYHLELNA KKAEVRTLVN NAVALTGSFV
     RLAKYGALTE DQAQGLALEI LGAARFDHGN YYFVDDKDGT IIQHANKALI GTNRSNTKDA
     YGTYIIRPML KAALAGHPIF HEYYIPKAGS KTPEAKISYM AKVPGWNWVI GTGMYVSDLR
     TSFWSNVARF VGIFVPVFLL FLVAMYFIQR NIAGILKAMT GAMARLSKGD LKAEVPYVAR
     ADEIGGMARA VEVFKAAGIE KARLEAEAAA SRAAREAEAA RSAAEREQAA QQLAFVVESI
     ATGLENLAAG RITYRLNTSF AAEYERLRTD FNAAMERLQD TMRVIAANTS AIRSGTGEIA
     AAADDLARRT EHQAATIEET AATLSEITET VSGTATHAAH AREAVSAAMA DAGRGGAVVA
     RAVAAMGEIE TSAEQIGNII GVIDEIAFQT NLLALNAGVE AARAGDAGRG FAVVASEVRA
     LAQRSADAAK EIKALISKSN QQVAAGVDQV GQTGKALERI VAQIAEINQV VSDIASGAQG
     NSARLLQVND AVSQMDQATQ QNAAMVEEST AASHNLAREV KQLAALIHRF DIEESAPAPV
     RSPAPAERPA AAPPARRMPE PTMADEGWEE F
//
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