ID U5WBG0_9ACTN Unreviewed; 515 AA.
AC U5WBG0;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE SubName: Full=Putative methyl-accepting chemotaxis protein {ECO:0000313|EMBL:AGZ46327.1};
GN ORFNames=AFR_40365 {ECO:0000313|EMBL:AGZ46327.1};
OS Actinoplanes friuliensis DSM 7358.
OC Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC Micromonosporaceae; Actinoplanes.
OX NCBI_TaxID=1246995 {ECO:0000313|EMBL:AGZ46327.1, ECO:0000313|Proteomes:UP000017746};
RN [1] {ECO:0000313|EMBL:AGZ46327.1, ECO:0000313|Proteomes:UP000017746}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 7358 {ECO:0000313|EMBL:AGZ46327.1,
RC ECO:0000313|Proteomes:UP000017746};
RX PubMed=24637369; DOI=10.1016/j.jbiotec.2014.03.011;
RA Ruckert C., Szczepanowski R., Albersmeier A., Goesmann A., Fischer N.,
RA Steinkamper A., Puhler A., Biener R., Schwartz D., Kalinowski J.;
RT "Complete genome sequence of the actinobacterium Actinoplanes friuliensis
RT HAG 010964, producer of the lipopeptide antibiotic friulimycin.";
RL J. Biotechnol. 178:41-42(2014).
CC -!- SIMILARITY: Belongs to the methyl-accepting chemotaxis (MCP) protein
CC family. {ECO:0000256|ARBA:ARBA00029447}.
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DR EMBL; CP006272; AGZ46327.1; -; Genomic_DNA.
DR AlphaFoldDB; U5WBG0; -.
DR STRING; 1246995.AFR_40365; -.
DR KEGG; afs:AFR_40365; -.
DR PATRIC; fig|1246995.3.peg.8169; -.
DR eggNOG; COG0840; Bacteria.
DR HOGENOM; CLU_000445_107_27_11; -.
DR Proteomes; UP000017746; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0003824; F:catalytic activity; IEA:UniProt.
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 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; PTHR32089:SF112; HEME-BASED AEROTACTIC TRANSDUCER HEMAT; 1.
DR PANTHER; PTHR32089; METHYL-ACCEPTING CHEMOTAXIS PROTEIN MCPB; 1.
DR Pfam; PF00672; HAMP; 1.
DR Pfam; PF00015; MCPsignal; 1.
DR PRINTS; PR00260; CHEMTRNSDUCR.
DR SMART; SM00304; HAMP; 1.
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|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000017746};
KW Transducer {ECO:0000256|ARBA:ARBA00023224, ECO:0000256|PROSITE-
KW ProRule:PRU00284}; Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 178..199
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 200..252
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 257..486
FT /note="Methyl-accepting transducer"
FT /evidence="ECO:0000259|PROSITE:PS50111"
SQ SEQUENCE 515 AA; 53205 MW; 654371B1034983FD CRC64;
MEMGIAKRLT LIVLVGALAI VGLTINTVSG QRSLVGQADL VRVLEAGLAA LNHLDTRQSE
LKVDGYRAAL GDDVTTDVAD DVVSATEAAD AVEAVGLPAD LAAEFATIRP NVDSFGTFMA
DFVKQAGAGG DAAEANRDQI AQRNNAVDDQ LGALNEKVAA AAEQERADMN STINRISLIT
YLFSGIGLLL LIGLSVPLAR SILRPVRRLG EVIDALAKGD LTQRSGITSR DEVGRMAVGL
DSALSSIHRS LSTIGQNAET LASSATELSA VAGQIAESAH DTDAQTSSAS NEAEEISRNV
QTVAAGSEEM GLSIREISRN TSEAAQIAAV AVTEAAQATE TIRQLGESSA EIGNVIKLIT
SIAEQTNLLA LNATIEAARA GDAGKGFAVV ASEVKDLAQE TARATEDIGS RVTAIQQDTS
GAVAVISRIS EVIARINDFQ TTIASAVEEQ TATTGEMSRS ISEVASGSSR IAANIADVST
ASGSAVHGVT QTRQASEEVA RTAEELRALV GAFKL
//
