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Database: UniProt
Entry: A0A1H9DA49_9GAMM
LinkDB: A0A1H9DA49_9GAMM
Original site: A0A1H9DA49_9GAMM 
ID   A0A1H9DA49_9GAMM        Unreviewed;       555 AA.
AC   A0A1H9DA49;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 17.
DE   SubName: Full=Methyl-accepting chemotaxis sensory transducer with Cache sensor {ECO:0000313|EMBL:SEQ10187.1};
GN   ORFNames=SAMN03080615_00426 {ECO:0000313|EMBL:SEQ10187.1};
OS   Amphritea atlantica.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC   Oceanospirillaceae; Amphritea.
OX   NCBI_TaxID=355243 {ECO:0000313|EMBL:SEQ10187.1, 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   -!- 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}.
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DR   EMBL; FOGB01000001; SEQ10187.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H9DA49; -.
DR   STRING; 355243.SAMN03080615_00426; -.
DR   OrthoDB; 6376221at2; -.
DR   Proteomes; UP000198749; Unassembled WGS sequence.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR   GO; GO:0006935; P:chemotaxis; IEA:UniProt.
DR   GO; GO:0007165; P:signal transduction; IEA:UniProtKB-KW.
DR   CDD; cd06225; HAMP; 1.
DR   CDD; cd11386; MCP_signal; 1.
DR   Gene3D; 1.10.287.950; Methyl-accepting chemotaxis protein; 1.
DR   Gene3D; 3.30.450.20; PAS domain; 1.
DR   InterPro; IPR003660; HAMP_dom.
DR   InterPro; IPR004089; MCPsignal_dom.
DR   InterPro; IPR033480; sCache_2.
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   Pfam; PF17200; sCache_2; 1.
DR   SMART; SM01049; Cache_2; 1.
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   Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Transducer {ECO:0000256|ARBA:ARBA00023224, ECO:0000256|PROSITE-
KW   ProRule:PRU00284};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        9..30
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        199..221
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          223..277
FT                   /note="HAMP"
FT                   /evidence="ECO:0000259|PROSITE:PS50885"
FT   DOMAIN          282..518
FT                   /note="Methyl-accepting transducer"
FT                   /evidence="ECO:0000259|PROSITE:PS50111"
SQ   SEQUENCE   555 AA;  60329 MW;  2EDE0831CF63771B CRC64;
     MTVSISKRLT IMGTAPVILL AVILLILTVF ENNELRHEQL QVTESKLLEM KRAELESLNK
     VALNSIKHIY DAGGELKDAL PILRALKYGK NGYFFGYTDK GERVFMGEMD KSIGKNFWDL
     QDSNGVYIIR ELVKAGKQGG GFVTYYFPKP GQDIAEAKLS YALYLDRWNL MIGAGFYLDD
     VKAILADVDT ASLNSLDTLL IYFALASVVL VVLAVIFSSV VKASIMRPLY SINESMKSLS
     TGEGDLTSRL KIDGDHELGD LAQSFNRFIE TLQKMVGEVI ALSAGVTQRS SAISKQMEQV
     SNLLHQQQVQ IEHSASAMSQ MSATAQDIAH NTAETANSTN ESRDNLNQAE GSVVELTGAV
     KTLADDVAGS NQAISTLENN VQDIISVVGV IQEIAEQTNL LALNAAIEAA RAGEQGRGFA
     VVADEVRTLA TRTQASTLQV HESIEKLKLA SSDAVKTMQH SFKQSDLAVT QSEKGMSELS
     KVSGHMDLIQ EMSVVIATAA EEQSQVCENL NQTVTEIAGH SEMSSQIARE NNQAVQDLAQ
     EAGKLQKLVG RFKVA
//
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