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Database: UniProt
Entry: A0A0F4R7W3_9GAMM
LinkDB: A0A0F4R7W3_9GAMM
Original site: A0A0F4R7W3_9GAMM 
ID   A0A0F4R7W3_9GAMM        Unreviewed;       519 AA.
AC   A0A0F4R7W3;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   SubName: Full=Chemotaxis protein {ECO:0000313|EMBL:KJZ16013.1};
GN   ORFNames=TW85_03825 {ECO:0000313|EMBL:KJZ16013.1};
OS   Marinomonas sp. S3726.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC   Oceanospirillaceae; Marinomonas.
OX   NCBI_TaxID=579484 {ECO:0000313|EMBL:KJZ16013.1, ECO:0000313|Proteomes:UP000033747};
RN   [1] {ECO:0000313|EMBL:KJZ16013.1, ECO:0000313|Proteomes:UP000033747}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=S3726 {ECO:0000313|EMBL:KJZ16013.1,
RC   ECO:0000313|Proteomes:UP000033747};
RX   PubMed=25879706; DOI=10.1186/s12864-015-1365-z;
RA   Machado H., Sonnenschein E.C., Melchiorsen J., Gram L.;
RT   "Genome mining reveals unlocked bioactive potential of marine Gram-negative
RT   bacteria.";
RL   BMC Genomics 16:158-158(2015).
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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KJZ16013.1}.
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DR   EMBL; JXYC01000004; KJZ16013.1; -; Genomic_DNA.
DR   RefSeq; WP_046015731.1; NZ_JXYC01000004.1.
DR   AlphaFoldDB; A0A0F4R7W3; -.
DR   PATRIC; fig|579484.3.peg.786; -.
DR   OrthoDB; 5675566at2; -.
DR   Proteomes; UP000033747; Unassembled WGS sequence.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
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   CDD; cd00130; PAS; 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; IPR004089; MCPsignal_dom.
DR   InterPro; IPR000014; PAS.
DR   InterPro; IPR035965; PAS-like_dom_sf.
DR   InterPro; IPR013655; PAS_fold_3.
DR   InterPro; IPR000727; T_SNARE_dom.
DR   NCBIfam; TIGR00229; sensory_box; 1.
DR   PANTHER; PTHR32089:SF112; HEME-BASED AEROTACTIC TRANSDUCER HEMAT; 1.
DR   PANTHER; PTHR32089; METHYL-ACCEPTING CHEMOTAXIS PROTEIN MCPB; 1.
DR   Pfam; PF00015; MCPsignal; 1.
DR   Pfam; PF08447; PAS_3; 1.
DR   PRINTS; PR00260; CHEMTRNSDUCR.
DR   SMART; SM00283; MA; 1.
DR   SMART; SM00091; PAS; 1.
DR   SUPFAM; SSF58104; Methyl-accepting chemotaxis protein (MCP) signaling domain; 1.
DR   SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 1.
DR   PROSITE; PS50111; CHEMOTAXIS_TRANSDUC_2; 1.
DR   PROSITE; PS50112; PAS; 1.
DR   PROSITE; PS50192; T_SNARE; 1.
PE   3: Inferred from homology;
KW   Methylation {ECO:0000256|ARBA:ARBA00022481};
KW   Reference proteome {ECO:0000313|Proteomes:UP000033747};
KW   Transducer {ECO:0000256|ARBA:ARBA00023224, ECO:0000256|PROSITE-
KW   ProRule:PRU00284}.
FT   DOMAIN          18..73
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          246..482
FT                   /note="Methyl-accepting transducer"
FT                   /evidence="ECO:0000259|PROSITE:PS50111"
FT   DOMAIN          433..482
FT                   /note="T-SNARE coiled-coil homology"
FT                   /evidence="ECO:0000259|PROSITE:PS50192"
SQ   SEQUENCE   519 AA;  56115 MW;  AF32FEC96A36D03D CRC64;
     MTAQSPQEYR FSEQDRLISA TDTKGYIVYC NDAFAAVSGY EREELIGQPH NLIRHEDMPK
     AAFTEMWRTL KEGKVWMGLV KNKRKNGDYY WVSAFVTPVY EGDKVVGYES VRINASEAEK
     TRATKVYKRL SQGKAARSLL HSLQIGLVKS LPMLVPGLAS AGLLYTTSGA GAAGIALAGT
     LIASVWQGLK AKSQWQQLCD MNQGTYSNAL VAQTYFDESG HQAKAKLAFA CEIARNRTSL
     TRIEDSAAGL GKIAHEAKDQ VNQTNVAIYQ QNTATQEVAS AIDQMASAIE EITNIVQSNT
     VNAQGALTHV DTGSQLATDA LQVIDKLSQS VEDIAITIKE LAQSTEEIGE AADLISMIAD
     QTNLLALNAA IEAARAGEHG RGFSVVADEV RSLSLKTRES TEKIHEVIQV LSSRAQSAVT
     VSQQGEEVAK QGVSIVGETR SSLNQINGAV KEILDMTLQI SASVEEQSAM TEHINQQVTD
     ISNGANHTKG IAEQTLASGV ELEETVGNVH SIIRRFSTH
//
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