ID A0A0F5ZZM2_9GAMM Unreviewed; 540 AA.
AC A0A0F5ZZM2;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=Chemotaxis protein {ECO:0000313|EMBL:KKD61211.1};
GN ORFNames=RN22_07000 {ECO:0000313|EMBL:KKD61211.1};
OS Grimontia sp. AD028.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Grimontia.
OX NCBI_TaxID=1581149 {ECO:0000313|EMBL:KKD61211.1, ECO:0000313|Proteomes:UP000033732};
RN [1] {ECO:0000313|EMBL:KKD61211.1, ECO:0000313|Proteomes:UP000033732}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AD028 {ECO:0000313|EMBL:KKD61211.1,
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:KKD61211.1}.
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DR EMBL; LASY01000028; KKD61211.1; -; Genomic_DNA.
DR RefSeq; WP_046303671.1; NZ_LASY01000028.1.
DR AlphaFoldDB; A0A0F5ZZM2; -.
DR PATRIC; fig|1581149.3.peg.1957; -.
DR OrthoDB; 9177152at2; -.
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; cd06225; HAMP; 1.
DR CDD; cd11386; MCP_signal; 1.
DR Gene3D; 6.10.340.10; -; 1.
DR Gene3D; 1.10.287.950; Methyl-accepting chemotaxis protein; 1.
DR InterPro; IPR004090; Chemotax_Me-accpt_rcpt.
DR InterPro; IPR003660; HAMP_dom.
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; PF00672; HAMP; 1.
DR Pfam; PF00015; MCPsignal; 1.
DR PRINTS; PR00260; CHEMTRNSDUCR.
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 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 12..31
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 187..207
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 209..262
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 267..503
FT /note="Methyl-accepting transducer"
FT /evidence="ECO:0000259|PROSITE:PS50111"
SQ SEQUENCE 540 AA; 57987 MW; 7D0F62E2643A1DD6 CRC64;
MLRKLTVSQK LFFGFGGILS LLVGMVAFVW IKLAFLQEVG IEVRTDDVPE AIGYLGLIDE
AGDVYRDSMG VINDVTGAKE DLKSNIKEYM DLIAHVRLLE TPGSEDFQRL AEIEEHMKAY
LAAFENSILP RVGNGVEMSD LVEELHDVYL MHLAPIEDIL DQVSSEEVAE TDKALGSLLE
AYEVMRMTLL SLAAVAILLS CGIAYLLSTS ITRRLTILNQ AAQRIANGEL SNESIEDKSG
DELASLAVSV NGMQASLVSL ISSIRGVTEE VHFSAKALST ISQDVVSGAS MQDEKATLIA
TASEELSLTI SEVANQGTAT FDEAKRSEES AHEGRRVIGE MVNSIQQVSV QMQEMSVSMR
ELGSHSEEIG NVIKVIQGIA EQTNLLALNA AIEAARAGEF GRGFAVVADE VRALAERTTQ
ATQEVSTIIQ SIQTGTQNAV TSTEENCGLV EIGVNHSESA VKALDDIFNG AASVQSMIST
IATAADEQTS VTREIASDIT AISDISSKSL DSAQQSADRI ASLDRKVDEL DALIGKFKVC
//
