ID F6IJ74_9SPHN Unreviewed; 616 AA.
AC F6IJ74;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 27-JUL-2011, sequence version 1.
DT 24-JAN-2024, entry version 46.
DE SubName: Full=Methyl-accepting chemotaxis protein {ECO:0000313|EMBL:CCA91700.1};
GN ORFNames=PP1Y_AT7624 {ECO:0000313|EMBL:CCA91700.1};
OS Novosphingobium sp. PP1Y.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Novosphingobium.
OX NCBI_TaxID=702113 {ECO:0000313|EMBL:CCA91700.1, ECO:0000313|Proteomes:UP000009242};
RN [1] {ECO:0000313|EMBL:CCA91700.1, ECO:0000313|Proteomes:UP000009242}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=sp. PP1Y {ECO:0000313|Proteomes:UP000009242};
RX PubMed=21685292; DOI=10.1128/JB.05349-11;
RA D'Argenio V., Petrillo M., Cantiello P., Naso B., Cozzuto L., Notomista E.,
RA Paolella G., Di Donato A., Salvatore F.;
RT "De novo sequencing and assembly of the whole genome of Novosphingobium sp.
RT strain PP1Y.";
RL J. Bacteriol. 193:4296-4296(2011).
CC -!- SIMILARITY: Belongs to the methyl-accepting chemotaxis (MCP) protein
CC family. {ECO:0000256|ARBA:ARBA00029447}.
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DR EMBL; FR856862; CCA91700.1; -; Genomic_DNA.
DR RefSeq; WP_013832116.1; NC_015580.1.
DR AlphaFoldDB; F6IJ74; -.
DR KEGG; npp:PP1Y_AT7624; -.
DR eggNOG; COG0840; Bacteria.
DR HOGENOM; CLU_000445_107_20_5; -.
DR Proteomes; UP000009242; Chromosome.
DR GO; GO:0016020; C: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; cd11386; MCP_signal; 1.
DR Gene3D; 6.10.340.10; -; 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 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 PRINTS; PR00260; CHEMTRNSDUCR.
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 Coiled coil {ECO:0000256|SAM:Coils}; Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000009242};
KW Transducer {ECO:0000256|PROSITE-ProRule:PRU00284};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 21..45
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 181..204
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 209..262
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 271..316
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 321..550
FT /note="Methyl-accepting transducer"
FT /evidence="ECO:0000259|PROSITE:PS50111"
FT REGION 574..598
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 89..116
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 616 AA; 65132 MW; A260A335E11EAFB0 CRC64;
MAFGSGPGTS WLRRQSINRR LTIQSITAGV LSLCLIATIV VGSGLSLATS KKDDKTSEQA
LSAALLEKDF ASLERDVFRH AAIGTEQTQK DWESNAEDLK ESIRNAQANL DGEEAKHAGD
VEAKAEAYID AVASTFAAGP ATPEGLDRIG ALGNGVDDGI EQIREPVIKR SEILNEEQRA
VTFWVLVISS AIAFGAGLIS YLLARAIRSS ISEELGTVRD SIAEIEAGRL NGHIEHLERQ
DEIGELARAA ARLRDTVKAK ERSDAEARDM IKHVGDNLGR LASGDLTIEV PELGASYAAL
RADFNKTVVR LREAMQSVSR STHAIRTGSM EISQASDDLA QRTEHHASEI GTAAGAVSEL
SRALQDTAQS AAEAHRGVDA AVNEARRGGE VVGQAVGAME QIEKSTAEIG NIIAVIDSIA
FQTNLLALNA GVEAARAGDA GKGFAVVANE VRGLAQRSAE AAKDVRTLIE TSSSQVAVGV
DMVRRTGEAL DSIIARIDNT TEVVTRISNA SSEQSEKLRQ TNDTISQMDV VTQQNAAMVE
ESTAAARSLA TEADNLAELV GTFRIGDASV VSFKASEGRS SPARAATPAP RRASAPMTVG
NTAVAQVVDD ADWSEF
//
