ID A0A0F5ZW65_9GAMM Unreviewed; 651 AA.
AC A0A0F5ZW65;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE SubName: Full=Chemotaxis protein {ECO:0000313|EMBL:KKD59200.1};
GN ORFNames=RN22_17075 {ECO:0000313|EMBL:KKD59200.1};
OS Grimontia sp. AD028.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Grimontia.
OX NCBI_TaxID=1581149 {ECO:0000313|EMBL:KKD59200.1, ECO:0000313|Proteomes:UP000033732};
RN [1] {ECO:0000313|EMBL:KKD59200.1, ECO:0000313|Proteomes:UP000033732}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AD028 {ECO:0000313|EMBL:KKD59200.1,
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:KKD59200.1}.
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DR EMBL; LASY01000077; KKD59200.1; -; Genomic_DNA.
DR RefSeq; WP_046306087.1; NZ_LASY01000077.1.
DR AlphaFoldDB; A0A0F5ZW65; -.
DR PATRIC; fig|1581149.3.peg.4337; -.
DR OrthoDB; 8724845at2; -.
DR Proteomes; UP000033732; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0006935; P:chemotaxis; IEA:UniProt.
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; IPR003660; HAMP_dom.
DR InterPro; IPR032255; HBM.
DR InterPro; IPR004089; MCPsignal_dom.
DR PANTHER; PTHR32089:SF122; ENERGY TAXIS MODULATING 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 SMART; SM00304; HAMP; 1.
DR SMART; SM01358; HBM; 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 Coiled coil {ECO:0000256|SAM:Coils}; 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 DOMAIN 297..351
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 356..592
FT /note="Methyl-accepting transducer"
FT /evidence="ECO:0000259|PROSITE:PS50111"
FT REGION 418..442
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 627..651
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 241..268
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 651 AA; 71444 MW; 17A9CE065B57D8E8 CRC64;
MRLALPQTIK AQLSSVVLLI LFSVAVFAIS FQRSFSELET LDGASVEILK SQTSVLMLRR
HEKDFMARKE AKYKDRFENE YGALTQKLLT AKAKLNALDM EGHEAIDAML YKLEKYHRDF
EALVDQRMEI GASFDSGLKG TAREASHRVE REIQKVENDM LYNKLLMLRR HEKDFLLRSD
TQYVDKFNAL MDELSPAIAT SDMPASNRLI METALREYHK TFNALAAGME DVGLTPQSGL
HGSLRASVQE AERQMKALSE DLVTAIDIRE KSVTKRLTLI GGALAIVVCL TLGLITRLVT
HKVSVANALM KKIAEGESSL RVRMNLSGKD ELSEMASYFN QFIGNLQHTM EKIAGISSEL
SSNARRSLTM ASDTAINAEK QRSESDSVST AMTEMTATSR EIAESVSTAA NVAKELQDSA
QTGRAVNSET SAKANQLSES MRSASDNMQR LNADSEEIGS VIDVIRSITE QTNLLALNAA
IEAARAGDQG RGFAVVADQV RELAMKTHQS TDEITKIIEQ LQGGIRHSVD LMNESSEMAS
ISVEQAREGA SVMAAMVSQI EDIAGQNLQI ATASEEQTVV TESVDRNIIA IVELAEHTAN
AAKKSNVSAS AIEQLANELD KLVGTFTGQS QPQQRQEKEN GEQVDLELAR A
//
