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Database: UniProt
Entry: A0A1H9JXW1_9GAMM
LinkDB: A0A1H9JXW1_9GAMM
Original site: A0A1H9JXW1_9GAMM 
ID   A0A1H9JXW1_9GAMM        Unreviewed;       531 AA.
AC   A0A1H9JXW1;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   SubName: Full=Methyl-accepting chemotaxis protein {ECO:0000313|EMBL:SEQ91657.1};
GN   ORFNames=SAMN03080615_03215 {ECO:0000313|EMBL:SEQ91657.1};
OS   Amphritea atlantica.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC   Oceanospirillaceae; Amphritea.
OX   NCBI_TaxID=355243 {ECO:0000313|EMBL:SEQ91657.1, ECO:0000313|Proteomes:UP000198749};
RN   [1] {ECO:0000313|Proteomes:UP000198749}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 18887 {ECO:0000313|Proteomes:UP000198749};
RA   Varghese N., Submissions S.;
RL   Submitted (OCT-2016) 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; FOGB01000011; SEQ91657.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H9JXW1; -.
DR   STRING; 355243.SAMN03080615_03215; -.
DR   OrthoDB; 2489132at2; -.
DR   Proteomes; UP000198749; 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   CDD; cd06225; HAMP; 1.
DR   CDD; cd11386; MCP_signal; 1.
DR   Gene3D; 3.30.450.290; -; 1.
DR   Gene3D; 1.10.8.500; HAMP domain in histidine kinase; 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; METHYL-ACCEPTING CHEMOTAXIS PROTEIN MCPB; 1.
DR   PANTHER; PTHR32089:SF119; METHYL-ACCEPTING CHEMOTAXIS PROTEIN TLPQ; 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   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        180..200
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          201..254
FT                   /note="HAMP"
FT                   /evidence="ECO:0000259|PROSITE:PS50885"
FT   DOMAIN          259..495
FT                   /note="Methyl-accepting transducer"
FT                   /evidence="ECO:0000259|PROSITE:PS50111"
SQ   SEQUENCE   531 AA;  57883 MW;  30164FDD3046FD5E CRC64;
     MAIQTKVNLS LAFVFLIVLI TSVSVIYRSE TNLSSDIALK NTQNTAEAYF DSINIMMLSG
     AMANRQTLQS KILGNPELTE ARIIRGEPVR SMYGEGTPDS HIQDDLDKRA MNGETIAVEL
     DDEKGHRMTV VRPMHASSDY KGTNCLQCHP VEEGTILGAV RVTYSFANID KHIFANIRNI
     ALVELGMFII ALFLVGWMIH RIVLKPINTM NDTIREIEQN ADLTQQLKIE SNDEIGQMSA
     SFNSMLRTFH DSIDHVVQSI AMLGQCSQQI KDVTELANIG TAKQISRAEA VTNAMIAMDG
     ATQNVSATAD VTIKASDKAL QETRSGVDIT TGTVKKIEAL QQQIKHATDV IVQLEQQSYN
     IDAVLSVIQD IAEQTNLLAL NAAIEAARAG EQGRGFAVVA DEVRTLSQRT QNATVEINGI
     IGSLQQNAKG AAQVMGQASA ATESNVKEIQ ETSAVLFNIQ KEMESIAETN HSISESVKQS
     SAATLEIEGA VNEINEGSDH AKERVVRLSA ISVQINNLAD ELEKRASQFK L
//
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