ID A0A1H6V3E6_9PSED Unreviewed; 437 AA.
AC A0A1H6V3E6;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE SubName: Full=Methyl-accepting chemotaxis sensory transducer with Pas/Pac sensor {ECO:0000313|EMBL:SEI99088.1};
GN ORFNames=SAMN03159495_1900 {ECO:0000313|EMBL:SEI99088.1};
OS Pseudomonas sp. NFR16.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=1566248 {ECO:0000313|EMBL:SEI99088.1, ECO:0000313|Proteomes:UP000199219};
RN [1] {ECO:0000313|EMBL:SEI99088.1, ECO:0000313|Proteomes:UP000199219}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NFR16 {ECO:0000313|EMBL:SEI99088.1,
RC ECO:0000313|Proteomes:UP000199219};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the methyl-accepting chemotaxis (MCP) protein
CC family. {ECO:0000256|ARBA:ARBA00029447}.
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DR EMBL; FNYJ01000002; SEI99088.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H6V3E6; -.
DR STRING; 1566248.SAMN03159495_1900; -.
DR OrthoDB; 9765776at2; -.
DR Proteomes; UP000199219; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:InterPro.
DR GO; GO:0006935; P:chemotaxis; IEA:UniProt.
DR GO; GO:0007165; P:signal transduction; IEA:UniProtKB-KW.
DR CDD; cd11386; MCP_signal; 1.
DR CDD; cd00130; PAS; 2.
DR Gene3D; 1.10.287.950; Methyl-accepting chemotaxis protein; 1.
DR Gene3D; 3.30.450.20; PAS domain; 2.
DR InterPro; IPR004089; MCPsignal_dom.
DR InterPro; IPR001610; PAC.
DR InterPro; IPR000014; PAS.
DR InterPro; IPR000700; PAS-assoc_C.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR013655; PAS_fold_3.
DR NCBIfam; TIGR00229; sensory_box; 2.
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 Pfam; PF08447; PAS_3; 2.
DR SMART; SM00283; MA; 1.
DR SMART; SM00086; PAC; 2.
DR SMART; SM00091; PAS; 2.
DR SUPFAM; SSF58104; Methyl-accepting chemotaxis protein (MCP) signaling domain; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 2.
DR PROSITE; PS50111; CHEMOTAXIS_TRANSDUC_2; 1.
DR PROSITE; PS50113; PAC; 2.
DR PROSITE; PS50112; PAS; 1.
PE 3: Inferred from homology;
KW Transducer {ECO:0000256|ARBA:ARBA00023224, ECO:0000256|PROSITE-
KW ProRule:PRU00284}.
FT DOMAIN 93..145
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 162..195
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 215..267
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 263..437
FT /note="Methyl-accepting transducer"
FT /evidence="ECO:0000259|PROSITE:PS50111"
SQ SEQUENCE 437 AA; 48808 MW; 591C1FF9B672970E CRC64;
MFFDSSKNRL IQTLQHTVSY QTSLLEAINR SMASIEFDLH GVVLSANDNF YRAMHYRPEQ
VIGKEHRIFC TDEYVRSSEY SQLWARLRTG EFVSATFQRV AGDGRAVWLE ASYNPIKDAE
GKVVKIVKYA VDVTEKLQNE RESQNKLQAI DRAMAVIEFG LDGQIIAANE NLLRLMGYSR
QELLGKNHRI LCPADLVNSG EYLDFWRRLN KGEFFSGQFK RIGKHGQTLW LEASYNPVYD
ACGKLCKVVK YASDVTARIE KHEQDSHSAA QAYHISVQTR KYAEQGTQVI QQAASEMRQI
SQNIDDSSRI IGQLGERSEQ ITAIVNTIHS IADQTNLLAL NAAIEAARAG DQGRGFAVVA
DEVRQLAGRT SRSTQEISEM IQVIQNETRQ AIVSMDNTRT NAAKGVDLAD QAGSAIVQIS
AGTNDAVDAV RMFAGKD
//
