ID W0LDF1_9GAMM Unreviewed; 641 AA.
AC W0LDF1;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 48.
DE SubName: Full=Chemotaxis protein {ECO:0000313|EMBL:AHG20317.1};
GN ORFNames=Z042_12230 {ECO:0000313|EMBL:AHG20317.1};
OS Chania multitudinisentens RB-25.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Chania.
OX NCBI_TaxID=1441930 {ECO:0000313|EMBL:AHG20317.1, ECO:0000313|Proteomes:UP000019030};
RN [1] {ECO:0000313|EMBL:AHG20317.1, ECO:0000313|Proteomes:UP000019030}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RB-25 {ECO:0000313|EMBL:AHG20317.1,
RC ECO:0000313|Proteomes:UP000019030};
RA Robson E.H.J.;
RT "Isolation of Serratia multitudinisentens RB-25 from Ex-Landfill site.";
RL Submitted (JAN-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:AHG20317.1, ECO:0000313|Proteomes:UP000019030}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RB-25 {ECO:0000313|EMBL:AHG20317.1,
RC ECO:0000313|Proteomes:UP000019030};
RA Chan K.-G.;
RL Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the methyl-accepting chemotaxis (MCP) protein
CC family. {ECO:0000256|ARBA:ARBA00029447}.
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DR EMBL; CP007044; AHG20317.1; -; Genomic_DNA.
DR RefSeq; WP_024912863.1; NZ_JAJC01000020.1.
DR AlphaFoldDB; W0LDF1; -.
DR STRING; 1441930.Z042_12230; -.
DR KEGG; sfo:Z042_12230; -.
DR PATRIC; fig|1441930.4.peg.2432; -.
DR eggNOG; COG0840; Bacteria.
DR HOGENOM; CLU_000445_107_16_6; -.
DR OrthoDB; 6167817at2; -.
DR Proteomes; UP000019030; 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:UniProtKB-KW.
DR GO; GO:0007165; P:signal transduction; IEA:UniProtKB-KW.
DR CDD; cd06225; HAMP; 1.
DR CDD; cd11386; MCP_signal; 1.
DR Gene3D; 1.20.1440.210; -; 1.
DR Gene3D; 1.10.287.950; Methyl-accepting chemotaxis protein; 1.
DR InterPro; IPR004090; Chemotax_Me-accpt_rcpt.
DR InterPro; IPR004091; Chemotax_Me-accpt_rcpt_Me-site.
DR InterPro; IPR003660; HAMP_dom.
DR InterPro; IPR032255; HBM.
DR InterPro; IPR004089; MCPsignal_dom.
DR PANTHER; PTHR43531:SF16; METHYL-ACCEPTING CHEMOTAXIS PROTEIN III; 1.
DR PANTHER; PTHR43531; PROTEIN ICFG; 1.
DR Pfam; PF00672; HAMP; 1.
DR Pfam; PF16591; HBM; 1.
DR Pfam; PF00015; MCPsignal; 1.
DR PRINTS; PR00260; CHEMTRNSDUCR.
DR SMART; SM00304; HAMP; 1.
DR SMART; SM01358; HBM; 1.
DR SMART; SM00283; MA; 1.
DR SUPFAM; SSF58104; Methyl-accepting chemotaxis protein (MCP) signaling domain; 1.
DR PROSITE; PS00538; CHEMOTAXIS_TRANSDUC_1; 1.
DR PROSITE; PS50111; CHEMOTAXIS_TRANSDUC_2; 1.
DR PROSITE; PS50885; HAMP; 1.
DR PROSITE; PS51753; HBM; 1.
PE 3: Inferred from homology;
KW Chemotaxis {ECO:0000256|ARBA:ARBA00022500};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000019030};
KW Transducer {ECO:0000256|PROSITE-ProRule:PRU00284};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 20..42
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 47..276
FT /note="HBM"
FT /evidence="ECO:0000259|PROSITE:PS51753"
FT DOMAIN 303..355
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 360..589
FT /note="Methyl-accepting transducer"
FT /evidence="ECO:0000259|PROSITE:PS50111"
SQ SEQUENCE 641 AA; 70040 MW; A34C847B58138E84 CRC64;
MRVLKAMAGK FIHLTVGKKL SLGFSLVLLL AIIIAGTGSY YLHLIKSRTE RIDFSSQITT
QISQAKYARA MFGQTYKIEH LDSNRTHIEN VVKLVNHALE LNWDPHSRNE LEKLKVLIGK
YQQQRDVFQA AVTKKDAIRA SWNMAEIQEE LSQVARQLNN SDLQLPIAQL NQKLTFIRFG
VRGLLLTPNN DVEAQVMNAI DDARSAANTL NQRLEEPLLQ PLLAALDEYR SRIAAYLPAY
ENEQKLSQQL SQTAQEIDAL TSVFMQDELK ETNGNIIAAQ WQMGITTVIA ILTGLLVSWR
ITLQITHPLQ NALELAKRIA TGDLRKMQAS SRRDELGQLL NAVAAMSQNL RDMIEKIQLG
VSQVSTAAGE IAAGNTDLSS RTEQQAAAVE ETAASMEQLT ATVKQNADNA HHANQLATDA
SQTAQQGGAL VNNVVSTMRD ISSSSQRIAE ITTLINGIAF QTNILALNAA VEAARAGEQG
RGFSVVASEV RNLAQRSAQA AKEIEGLIAE SVSRVQTGTA LVEDTGNTME QIVRSVTHVR
DIMAEIAAAS DEQTRGIAQI GQAIVEMDHT TQQNAALVEQ SAAAADSLEE QAEMLLQSVS
VFRLAERNEL AEAKNAVIKS SQATKVRETT ASAAENNWTT F
//
