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Database: UniProt
Entry: A0A2S2E639_9ALTE
LinkDB: A0A2S2E639_9ALTE
Original site: A0A2S2E639_9ALTE 
ID   A0A2S2E639_9ALTE        Unreviewed;       647 AA.
AC   A0A2S2E639;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, sequence version 1.
DT   27-MAR-2024, entry version 18.
DE   SubName: Full=Methyl-accepting chemotaxis protein NahY {ECO:0000313|EMBL:AWL13118.1};
GN   ORFNames=HMF8227_02666 {ECO:0000313|EMBL:AWL13118.1};
OS   Saliniradius amylolyticus.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC   Alteromonadaceae; Saliniradius.
OX   NCBI_TaxID=2183582 {ECO:0000313|EMBL:AWL13118.1, ECO:0000313|Proteomes:UP000245728};
RN   [1] {ECO:0000313|EMBL:AWL13118.1, ECO:0000313|Proteomes:UP000245728}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HMF8227 {ECO:0000313|EMBL:AWL13118.1,
RC   ECO:0000313|Proteomes:UP000245728};
RA   Kang H., Kang J., Cha I., Kim H., Joh K.;
RT   "Salinimonas sp. HMF8227 Genome sequencing and assembly.";
RL   Submitted (MAY-2018) 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; CP029347; AWL13118.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2S2E639; -.
DR   KEGG; salh:HMF8227_02666; -.
DR   OrthoDB; 2489132at2; -.
DR   Proteomes; UP000245728; Chromosome.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR   GO; GO:0004888; F:transmembrane signaling receptor activity; IEA:InterPro.
DR   GO; GO:0006935; P:chemotaxis; IEA:UniProtKB-KW.
DR   GO; GO:0007165; P:signal transduction; IEA:UniProtKB-KW.
DR   CDD; cd06225; HAMP; 1.
DR   CDD; cd11386; MCP_signal; 1.
DR   CDD; cd18773; PDC1_HK_sensor; 1.
DR   CDD; cd12912; PDC2_MCP_like; 1.
DR   Gene3D; 1.10.287.950; Methyl-accepting chemotaxis protein; 1.
DR   Gene3D; 3.30.450.20; PAS domain; 1.
DR   InterPro; IPR004090; Chemotax_Me-accpt_rcpt.
DR   InterPro; IPR033479; dCache_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; PF02743; dCache_1; 1.
DR   Pfam; PF00672; HAMP; 1.
DR   Pfam; PF00015; MCPsignal; 1.
DR   PRINTS; PR00260; CHEMTRNSDUCR.
DR   SMART; SM00304; HAMP; 2.
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   Chemotaxis {ECO:0000256|ARBA:ARBA00022500};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000245728};
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        12..31
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        292..315
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          316..370
FT                   /note="HAMP"
FT                   /evidence="ECO:0000259|PROSITE:PS50885"
FT   DOMAIN          375..611
FT                   /note="Methyl-accepting transducer"
FT                   /evidence="ECO:0000259|PROSITE:PS50111"
SQ   SEQUENCE   647 AA;  70019 MW;  1F3BB6D3E4F757D2 CRC64;
     MSIIQQLTIK NAVAGAMVIA LLSTTALSTL INISQFSSMF YDVTEQEHLP NLVGRAKAQI
     LERLQQPIAL SEAIANNTYV HRWVAQGEPD AQRGELIEFL NDFVRDYNAV AAFWVSMPTG
     NYYNQDGLFK QVSRTAERDQ WFYDFMASGK RTELALDVSE STGDLIVFIN ARVTSRSNGD
     IGAAGLGFDV SDISKLVNQT QVGENGYMFL LDEQGTIAAH RNNALIGKSV KAVSQYRNIH
     SEILRSSGEF RVFQRDVGDI EQYIAVTELE QQGWKIVTLL PRSEVSGQVN GIIGLSTAIT
     LVIAALFIGL AFVFARKVSA SVQSVADSLK RMSGDGGDLT QRLDDSADNE LGQLAAGFNA
     ILAKLADLVS EIQSSEQVIT QGMEKLEQGA NQTVSDSSSQ KAQTEQVATA MNQMGQTISE
     VSSVAHKTAT DTEQAVSEVN QTNTTMLDVA TTMHNLATAM QSTEQIMSEL ANQAESINSV
     VDVISGISEQ TNLLALNAAI EAARAGEQGR GFAVVADEVR TLASRTQDST AEIRDQIEQL
     QSSAIQSKQA IVQGAEQSAD LSQQAQSCTD SLSAVKAKFE QINDGNHQVA SATEQQASVV
     EHINESAQII ADTASSIYDN AETDLAEIKR LKEQALHMQA VVRQFKV
//
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