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
//