ID A6D648_9VIBR Unreviewed; 478 AA.
AC A6D648;
DT 24-JUL-2007, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2007, sequence version 1.
DT 03-MAY-2023, entry version 49.
DE SubName: Full=Methyl-accepting chemotaxis protein {ECO:0000313|EMBL:EDL51949.1};
GN ORFNames=VSAK1_15312 {ECO:0000313|EMBL:EDL51949.1};
OS Vibrio mediterranei AK1.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=391591 {ECO:0000313|EMBL:EDL51949.1, ECO:0000313|Proteomes:UP000003769};
RN [1] {ECO:0000313|EMBL:EDL51949.1, ECO:0000313|Proteomes:UP000003769}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AK1 {ECO:0000313|EMBL:EDL51949.1,
RC ECO:0000313|Proteomes:UP000003769};
RA Rosenberg E., Ferriera S., Johnson J., Kravitz S., Beeson K., Sutton G.,
RA Rogers Y.-H., Friedman R., Frazier M., Venter J.C.;
RL Submitted (JUN-2007) 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:EDL51949.1}.
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DR EMBL; ABCH01000042; EDL51949.1; -; Genomic_DNA.
DR RefSeq; WP_006074372.1; NZ_ABCH01000042.1.
DR AlphaFoldDB; A6D648; -.
DR Proteomes; UP000003769; 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; 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:SF65; CHEMOTAXIS SIGNAL TRANSDUCTION SYSTEM METHYL ACCEPTING SENSORY TRANSDUCER; 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 133..158
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 160..201
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 206..442
FT /note="Methyl-accepting transducer"
FT /evidence="ECO:0000259|PROSITE:PS50111"
FT REGION 250..269
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 478 AA; 51357 MW; 96ED56CD1E8886AF CRC64;
MREVKFRKID ALFIKMSIND KMWVLFALFF AALTFSAVSR YQDSVSNAEQ QAIASAEAKL
SGYLEVSSAT GNSSILKNFN VIESTSQASS INNGQVTATA RGLDGKNYSL TTSASIQIDN
AKSQALTSLA LTYLWLLPFS IFSYWLATFL GGALFTLYST TQKIADGDLT SRLNFVAGRD
EFGTIGVALD RAMDTLTELV TTVKSSATSL EETASSFQEE MAKSNNQINN QYASLDSVAT
AMEQMTASAQ EVSNISRQSN EQAEEDTKQV ELSYQRVQQA IGDINQLSAF IEEASHSVAA
LTDNTTQINE VITTINAISE QTNLLALNAA IEAARAGEQG RGFAVVADEV RTLAGRTQTA
TVEIQAMIEK LQSESQNIAA ITQQTVEQAE SSSALISEIG HDVNSIADSS RAVMDMSTQI
STSAAEQSAV AAEIAAELSD IRVQSGTIRE VAEQSEVGVS NLTKATITLG EVLTRYRT
//
