ID A0A0X1T8X2_PSEAA Unreviewed; 524 AA.
AC A0A0X1T8X2;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=Chemotaxis protein {ECO:0000313|EMBL:AMB88403.1};
GN ORFNames=AWM79_23670 {ECO:0000313|EMBL:AMB88403.1};
OS Pseudomonas agarici.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=46677 {ECO:0000313|EMBL:AMB88403.1, ECO:0000313|Proteomes:UP000063229};
RN [1] {ECO:0000313|EMBL:AMB88403.1, ECO:0000313|Proteomes:UP000063229}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCPPB 2472 {ECO:0000313|EMBL:AMB88403.1,
RC ECO:0000313|Proteomes:UP000063229};
RA McClelland M., Jain A., Saraogi P., Mendelson R., Westerman R.,
RA SanMiguel P., Csonka L.;
RL Submitted (JAN-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000256|ARBA:ARBA00004429}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004429}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the methyl-accepting chemotaxis (MCP) protein
CC family. {ECO:0000256|ARBA:ARBA00029447}.
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DR EMBL; CP014135; AMB88403.1; -; Genomic_DNA.
DR RefSeq; WP_051000694.1; NZ_JACAQG010000014.1.
DR AlphaFoldDB; A0A0X1T8X2; -.
DR STRING; 46677.AWM79_23670; -.
DR Proteomes; UP000063229; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0006935; P:chemotaxis; IEA:UniProtKB-KW.
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 Gene3D; 3.30.450.20; PAS domain; 1.
DR InterPro; IPR003660; HAMP_dom.
DR InterPro; IPR004089; MCPsignal_dom.
DR InterPro; IPR033480; sCache_2.
DR InterPro; IPR000727; T_SNARE_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 Pfam; PF17200; sCache_2; 1.
DR SMART; SM01049; Cache_2; 1.
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.
DR PROSITE; PS50192; T_SNARE; 1.
PE 3: Inferred from homology;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Chemotaxis {ECO:0000256|ARBA:ARBA00022500};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Methylation {ECO:0000256|ARBA:ARBA00022481};
KW Reference proteome {ECO:0000313|Proteomes:UP000063229};
KW Transducer {ECO:0000256|ARBA:ARBA00023224, ECO:0000256|PROSITE-
KW ProRule:PRU00284};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 170..191
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 193..247
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 252..488
FT /note="Methyl-accepting transducer"
FT /evidence="ECO:0000259|PROSITE:PS50111"
FT DOMAIN 447..487
FT /note="T-SNARE coiled-coil homology"
FT /evidence="ECO:0000259|PROSITE:PS50192"
SQ SEQUENCE 524 AA; 57237 MW; 223609146FF69D7D CRC64;
MLMLIALSAL MLYQIRDDLF NAKTLKTHHV VETVSGILRY YHAKEISGEL TREEAQKQAS
IMVNGLRYNQ TDYFVLLDLQ GTMLMHPTNP KLQGVNMLET KDPEGRLYIR EMVDLAKYKG
QGKVDYFWPK PGSDEPLPKV SYVELFKPWG WIITSGAYVN DVLLEFRGKI INALGNLAIV
GILLAVLVTL ISRSISLPLT AIVDAMANIA TGDADLTRNL DNKGHDELTA LGQHFNSFMG
NLNRVISQTR QVAGALDHAS LSLGDVASTG QRQSQQQSQQ MEQVATAINE VSYAVQDVAK
GAKHAANEVL QAEEQALQGQ HSIESSLHQT DRLSETIDQA VVVIQRLDQE SSQIGRVLEV
IRAIAEQTNL LALNAAIEAA RAGEQGRGFA VVADEVRLLA QRTQTSTAEI QFMIEQLQNN
SQAAVKAINA SSMASQKTVE LARLAGQNLN QITSSLRNIS GLNASIAGAT LQQSQVVDEI
NKSVTQAASL AHDGAALADR SNEASRHLEQ LKGDLNQLLG RFRV
//
