ID A0A0M2M023_9SPHN Unreviewed; 513 AA.
AC A0A0M2M023;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=Methyl-accepting transducer domain-containing protein {ECO:0000259|PROSITE:PS50111};
GN ORFNames=XM50_03045 {ECO:0000313|EMBL:KKI21259.1};
OS Sphingomonas sp. Ag1.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingomonas.
OX NCBI_TaxID=1642949 {ECO:0000313|EMBL:KKI21259.1, ECO:0000313|Proteomes:UP000033997};
RN [1] {ECO:0000313|EMBL:KKI21259.1, ECO:0000313|Proteomes:UP000033997}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ag1 {ECO:0000313|EMBL:KKI21259.1,
RC ECO:0000313|Proteomes:UP000033997};
RA Pei D., Yu W., Kukutla P., Xu J.;
RT "Draft Genome Sequences of Sphingomonas sp. Ag1 from Mosquito Anopheles
RT gambiae.";
RL Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases.
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:KKI21259.1}.
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DR EMBL; LAZX01000076; KKI21259.1; -; Genomic_DNA.
DR RefSeq; WP_046407285.1; NZ_LAZX01000076.1.
DR AlphaFoldDB; A0A0M2M023; -.
DR STRING; 1642949.XM50_03045; -.
DR PATRIC; fig|1642949.3.peg.3341; -.
DR OrthoDB; 354287at2; -.
DR Proteomes; UP000033997; Unassembled WGS sequence.
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 Gene3D; 1.10.287.950; Methyl-accepting chemotaxis protein; 1.
DR InterPro; IPR004090; Chemotax_Me-accpt_rcpt.
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; PF00015; MCPsignal; 1.
DR PRINTS; PR00260; CHEMTRNSDUCR.
DR SMART; SM00283; MA; 1.
DR SUPFAM; SSF58104; Methyl-accepting chemotaxis protein (MCP) signaling domain; 1.
DR PROSITE; PS50111; CHEMOTAXIS_TRANSDUC_2; 1.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils}; Membrane {ECO:0000256|SAM:Phobius};
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 12..32
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 38..57
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 64..85
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 113..132
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 144..162
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 251..487
FT /note="Methyl-accepting transducer"
FT /evidence="ECO:0000259|PROSITE:PS50111"
FT COILED 200..228
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 513 AA; 53409 MW; 95E790C5B8D6B590 CRC64;
MSSLDNLRMR GIRVIAAVGW LCLPLLLIWG AAMNAPGTGL AIAAAAMVNI IPTALAVRGR
HDLAARMSCG VLAAAMPAIY VYLLAGSAWQ MDGHMYFFVA LAMIAVLCDW RPLALAAILI
ALHHLVLSYV LPNWVFENGG ALDRVLFHAL AVVLEFAALT YLTTRLRILI VAQDVARQEG
ERLLALAEVE RGRAVAALAA AQAADERSQS ERQRREAAEA RLESERRSAL MALADDFERS
VAGVAVAIEG ASATLEGSAA TLTRIAAEAG RQASEVAVGA HQAAGATQDV ADAVHRLTDS
IGEIAESAHA QATLTGDVQR NAEQGKAAVL DLAARAGDIN GLVGEIHEIA TRTNLLALNA
TIEAARAGDA GRGFAVVAGE VKQLAGGTAR ASEKIVSLIG SVRHGVDSTE ASIVGAADAV
CRVAAAADAI KGAVSGQRGV AGQIERTAHE AARGVDMIEQ RIAQVAEAAN EADVLSQQVR
EAAGALSDQA RRLRRSTDGF VEQLRTGKRA VAA
//
