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Database: UniProt
Entry: A0A1G9YD85_9BACI
LinkDB: A0A1G9YD85_9BACI
Original site: A0A1G9YD85_9BACI 
ID   A0A1G9YD85_9BACI        Unreviewed;       621 AA.
AC   A0A1G9YD85;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   SubName: Full=Methyl-accepting chemotaxis protein {ECO:0000313|EMBL:SDN07034.1};
GN   ORFNames=SAMN05518871_103205 {ECO:0000313|EMBL:SDN07034.1};
OS   Psychrobacillus sp. OK028.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Psychrobacillus.
OX   NCBI_TaxID=1884359 {ECO:0000313|EMBL:SDN07034.1, ECO:0000313|Proteomes:UP000198927};
RN   [1] {ECO:0000313|Proteomes:UP000198927}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OK028 {ECO:0000313|Proteomes:UP000198927};
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; FNHY01000003; SDN07034.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1G9YD85; -.
DR   STRING; 1884359.SAMN05518871_103205; -.
DR   Proteomes; UP000198927; Unassembled WGS sequence.
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:InterPro.
DR   GO; GO:0007165; P:signal transduction; IEA:UniProtKB-KW.
DR   CDD; cd06225; HAMP; 1.
DR   Gene3D; 6.10.340.10; -; 1.
DR   Gene3D; 1.10.287.950; Methyl-accepting chemotaxis protein; 1.
DR   InterPro; IPR007891; CHASE3.
DR   InterPro; IPR004090; Chemotax_Me-accpt_rcpt.
DR   InterPro; IPR003660; HAMP_dom.
DR   InterPro; IPR004089; MCPsignal_dom.
DR   PANTHER; PTHR32089:SF92; LYSOZYME-LIKE PROTEIN-RELATED; 1.
DR   PANTHER; PTHR32089; METHYL-ACCEPTING CHEMOTAXIS PROTEIN MCPB; 1.
DR   Pfam; PF05227; CHASE3; 1.
DR   Pfam; PF00015; MCPsignal; 1.
DR   PRINTS; PR00260; CHEMTRNSDUCR.
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}; Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        60..81
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        239..264
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          262..316
FT                   /note="HAMP"
FT                   /evidence="ECO:0000259|PROSITE:PS50885"
FT   DOMAIN          335..571
FT                   /note="Methyl-accepting transducer"
FT                   /evidence="ECO:0000259|PROSITE:PS50111"
SQ   SEQUENCE   621 AA;  68398 MW;  0BBC8C905DBB641A CRC64;
     MRNSISNKLK SMKFPKIKTP KKNLGNPQRN KVTSLFKKSK NKDKQLKLNH STKASFLHSI
     RGRVLIIFTV LILVLISMLV LTSTKMFSAQ QALEKFTNVD VKEQMMVNQI ATDIAQLANA
     EQSYIITGKN NYMASYRKYK DSTTTNIKAL YKTYENRPDE LQKIQSIDQF FTTYLQYSDR
     VIKIRDEKGL ESAQKLVNTG NGKTAMSYVD VHIAAMNELL EKNNTDQIAL LKKENTTSLI
     IFIALTIFSV ILTLSFGILL FYSIKRNTNA INRSILDIAQ AGGDLTRRVK VRSKDEFSEI
     ANSTNVLIAS IADLVRRVRE LTVNVSASGQ ELMASSDETA LTIQSIADST NEIAAGSDQT
     LRSMTEAIQK MNSLEEATRY LNNDAQSVKA ATDQMIQAAQ KGGESVQHSS NVMMSIEETM
     ANTTQTVESL GTKSNEITSI IKTITTIAEQ TNLLALNAAI EAARAGEHGR GFAVVADEVR
     KLAEQSQKAA KEVTGIVTSI QSEVTSIVKQ NHEGVESVIR GVEVANETNT SLDEIIKQTN
     ETISIIDKMV KQIEETLNFS QEVAASFIEV TQIAENTASN TETSAAAAEQ GSAAMQEINA
     SAVELSHQAD ELSKVVNEFK L
//
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