ID A0A2K4GAA8_9PSED Unreviewed; 540 AA.
AC A0A2K4GAA8;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=Methyl-accepting chemotaxis protein {ECO:0000313|EMBL:POA20552.1};
GN ORFNames=C1886_08185 {ECO:0000313|EMBL:POA20552.1};
OS Pseudomonas sp. FW300-N1A1.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=2075555 {ECO:0000313|EMBL:POA20552.1, ECO:0000313|Proteomes:UP000236411};
RN [1] {ECO:0000313|EMBL:POA20552.1, ECO:0000313|Proteomes:UP000236411}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FW300-N1A1 {ECO:0000313|EMBL:POA20552.1,
RC ECO:0000313|Proteomes:UP000236411};
RA Spencer S.J., Aaring A.B., Hendricks A., Penterman J., Chakraborty R.,
RA Alm E.J.;
RT "Whole genome sequencing of deep branching strains shows evolution and
RT exchange across a contaminated watershed.";
RL Submitted (JAN-2018) 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:POA20552.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; PPSF01000013; POA20552.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2K4GAA8; -.
DR Proteomes; UP000236411; 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 Gene3D; 1.10.287.950; Methyl-accepting chemotaxis protein; 1.
DR InterPro; IPR004090; Chemotax_Me-accpt_rcpt.
DR InterPro; IPR003660; HAMP_dom.
DR InterPro; IPR024478; HlyB_4HB_MCP.
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; PF12729; 4HB_MCP_1; 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..32
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 189..210
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 211..263
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 268..504
FT /note="Methyl-accepting transducer"
FT /evidence="ECO:0000259|PROSITE:PS50111"
SQ SEQUENCE 540 AA; 58527 MW; EFF842FDB77DAB2D CRC64;
MKNWTLRQRI LASFAVIIAI MFLMVVVSYS RLLKIEASEN SVRDDAVPGL YYSSMIRSAW
VDSYLQTQKM LGLEEGQGVT AENVAEFESY EQHLQTLMAD YAATIHGRED RKEFDLFEKA
HQNYAIILAS VLELHRNNKE AEATKMFTEQ LTPAWTAGRV KLNEIIGENK VVADHATAAI
DDAVVAAKIS MGLSLLVAIV VAGLCGLLLM RAIMSPMNRI VNILETMRTG DLSNRLNLDR
KDEFGAVETG FNDMMTELTS LVSQAQRSSV QVTTSVTEIA ATSKQQQATA TETAATTTEI
GATSREIAAT SRDLVRTMTE VSTAADQASV LAGSGQQGLA RMEDTMHSVM GAADLVNAKL
AILNEKAGNI NQVVVTIVKV ADQTNLLSLN AAIEAEKAGE YGRGFAVVAT EVRRLADQTA
VATYDIEQMV REIQSAVSAG VMGMDKFSEE VRRGMSEVQQ VGEQLSQIIH QVQALAPRVL
MVNEGMQAQA TGAEQINHAL VQLGDASGQT VESLRQASFA IDELSQVAVG LRSGVSRFKV
//
