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Database: UniProt
Entry: S6HLM7_9GAMM
LinkDB: S6HLM7_9GAMM
Original site: S6HLM7_9GAMM 
ID   S6HLM7_9GAMM            Unreviewed;       577 AA.
AC   S6HLM7;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   27-MAR-2024, entry version 34.
DE   RecName: Full=Methyl-accepting chemotaxis protein {ECO:0008006|Google:ProtNLM};
GN   ORFNames=OFPI_22280 {ECO:0000313|EMBL:EPJ49857.1};
OS   Osedax symbiont Rs2.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC   Oceanospirillaceae.
OX   NCBI_TaxID=1330035 {ECO:0000313|EMBL:EPJ49857.1, ECO:0000313|Proteomes:UP000014830};
RN   [1] {ECO:0000313|EMBL:EPJ49857.1, ECO:0000313|Proteomes:UP000014830}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Rs2 {ECO:0000313|Proteomes:UP000014830};
RA   Yi H., Goffredi S.;
RT   "Comparative genomics of two novel heterotrophic symbionts of deep-sea
RT   Osedax worms: functional variation and environmental selection.";
RL   Submitted (MAY-2013) 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:EPJ49857.1}.
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DR   EMBL; ASZI01000170; EPJ49857.1; -; Genomic_DNA.
DR   AlphaFoldDB; S6HLM7; -.
DR   Proteomes; UP000014830; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0006935; P:chemotaxis; IEA:UniProt.
DR   GO; GO:0007165; P:signal transduction; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.287.950; Methyl-accepting chemotaxis protein; 1.
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; PF00015; MCPsignal; 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   Reference proteome {ECO:0000313|Proteomes:UP000014830};
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        14..36
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        226..249
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          247..300
FT                   /note="HAMP"
FT                   /evidence="ECO:0000259|PROSITE:PS50885"
FT   DOMAIN          305..541
FT                   /note="Methyl-accepting transducer"
FT                   /evidence="ECO:0000259|PROSITE:PS50111"
SQ   SEQUENCE   577 AA;  63382 MW;  6C37985A35A32F23 CRC64;
     MISWLRRFNV TTRIMSLACF LVIVMVSQAA FFMVGLDNSK QRSELQLIKV AEENQLIENE
     AKQFVARAKV QKLQQQAQQV QKTFSDMLFW YFDGIVTEYY ESLTKATESA DLLQQQLNAL
     TSDSQSGTQV KQIMDTLVEY RELMNTAVGY YQQGKDNLAE SEIGDANLEA KNLNEQLLVL
     ANMIQTRLAH ADTELVAALE KTLAASKVVE QLSEQASEQV DRDLKVLWLI LLLTLPVAIG
     VATAVIMSIT RPLSVLKHQL LAIEQNSDLT QMLSLDGRDE IRDMSEATQN LLLKLRSTLD
     QVGLLANELN EAAKKGYSVS LDTLKQSTEQ QLQSAGIAAA ATELGASSED ISKTADQGLI
     LVKEVSKAAN EGQLDVQATA KTMHQLSAQF DGVESSVSEL VQHSSAIGQV LDVIRGIADQ
     TNLLALNAAI EAARAGDQGR GFAVVADEVR TLAQRPSQST DEIQKMVEAL QQHSKVASSS
     LESNRKHVDD SVKLSEQAET SLVRIIAELV ELESTNQVIA SITNEQQNAV TEVDENVQKI
     RALACNVEEQ AKDSSGVSES LTDMADKLQQ ELKVFRR
//
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