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Database: UniProt
Entry: A0A0F6A0G1_9GAMM
LinkDB: A0A0F6A0G1_9GAMM
Original site: A0A0F6A0G1_9GAMM 
ID   A0A0F6A0G1_9GAMM        Unreviewed;       552 AA.
AC   A0A0F6A0G1;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   SubName: Full=Chemotaxis protein {ECO:0000313|EMBL:KKD61506.1};
GN   ORFNames=RN22_05455 {ECO:0000313|EMBL:KKD61506.1};
OS   Grimontia sp. AD028.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Grimontia.
OX   NCBI_TaxID=1581149 {ECO:0000313|EMBL:KKD61506.1, ECO:0000313|Proteomes:UP000033732};
RN   [1] {ECO:0000313|EMBL:KKD61506.1, ECO:0000313|Proteomes:UP000033732}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AD028 {ECO:0000313|EMBL:KKD61506.1,
RC   ECO:0000313|Proteomes:UP000033732};
RA   Adrian T.-G.-S., Chan K.-G.;
RT   "Genome sequencing of Grimontia sp. AD028.";
RL   Submitted (APR-2015) 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:KKD61506.1}.
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DR   EMBL; LASY01000021; KKD61506.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0F6A0G1; -.
DR   PATRIC; fig|1581149.3.peg.1619; -.
DR   OrthoDB; 7054443at2; -.
DR   Proteomes; UP000033732; Unassembled WGS sequence.
DR   GO; GO:0016020; C: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; cd11386; MCP_signal; 1.
DR   Gene3D; 1.10.287.950; Methyl-accepting chemotaxis protein; 1.
DR   InterPro; IPR004090; Chemotax_Me-accpt_rcpt.
DR   InterPro; IPR004089; MCPsignal_dom.
DR   PANTHER; PTHR32089:SF112; HEME-BASED AEROTACTIC TRANSDUCER HEMAT; 1.
DR   PANTHER; PTHR32089; METHYL-ACCEPTING CHEMOTAXIS PROTEIN MCPB; 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.
PE   3: Inferred from homology;
KW   Membrane {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        7..27
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        200..221
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          281..517
FT                   /note="Methyl-accepting transducer"
FT                   /evidence="ECO:0000259|PROSITE:PS50111"
SQ   SEQUENCE   552 AA;  59583 MW;  1796A9969CF0B456 CRC64;
     MTIKQRLTMF VALVCGIQIL VGAFVFYKLA YIESHVQGVA HRDIPVLESL SKATEHQVEQ
     RVHYNKAFRY AHEIGKEPNA QENYDKEKAY FYDLGAKVGE DWTKIETLLA DGATNGTAEE
     QVAFAAASVK LADLEALHAK WMIHVEDVFK ELEGRHYHEA EVLDVVVGEE AETTTKMVDS
     LLTDVGKFTE AAVIDIEEKA VVLEFVVIAS VIVALIVAII MSKMILNRIY EGLNKVSAAL
     SVQADGDFSK PTVVDEPGII GELQKNLEGT RQSTNGMIAK VAQEVSDAVN LLDEAAQAVK
     RNSDAQSGEI LQVATAVNEM SATAQEIANN ATQTQQATEE ASGKSSECMR INDEAVSQTQ
     QLIESLTQSS AALTELEKNS ANITSVLDVI KGIAEQTNLL ALNAAIEAAR AGEQGRGFAV
     VADEVRSLAQ RTHDSTSEIE TMIAQLTSVT KEAVDTMQQS CEMGDKTIEL SHQSADLLNQ
     SSEATSRVTD MNLQVASAAD EQNGVVEEVN VNVSKISDMA NESAHQVAGL VNATDKLNVI
     AKNLRVSVGM AS
//
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