ID A0A0X3UME4_9ACTN Unreviewed; 528 AA.
AC A0A0X3UME4;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=Chemotaxis protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=ADL15_17095 {ECO:0000313|EMBL:KUL33715.1};
OS Actinoplanes awajinensis subsp. mycoplanecinus.
OC Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC Micromonosporaceae; Actinoplanes.
OX NCBI_TaxID=135947 {ECO:0000313|EMBL:KUL33715.1, ECO:0000313|Proteomes:UP000053244};
RN [1] {ECO:0000313|EMBL:KUL33715.1, ECO:0000313|Proteomes:UP000053244}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL B-16712 {ECO:0000313|EMBL:KUL33715.1,
RC ECO:0000313|Proteomes:UP000053244};
RA Gilbert D.G.;
RL Submitted (OCT-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:KUL33715.1}.
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DR EMBL; LLZH01000134; KUL33715.1; -; Genomic_DNA.
DR RefSeq; WP_067691518.1; NZ_LLZH01000134.1.
DR AlphaFoldDB; A0A0X3UME4; -.
DR OrthoDB; 1115140at2; -.
DR Proteomes; UP000053244; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0003824; F:catalytic activity; IEA:UniProt.
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; IPR007891; CHASE3.
DR InterPro; IPR004090; Chemotax_Me-accpt_rcpt.
DR InterPro; IPR003660; HAMP_dom.
DR InterPro; IPR004089; MCPsignal_dom.
DR PANTHER; PTHR32089:SF112; HEME-BASED AEROTACTIC TRANSDUCER HEMAT; 1.
DR PANTHER; PTHR32089; METHYL-ACCEPTING CHEMOTAXIS PROTEIN MCPB; 1.
DR Pfam; PF05227; CHASE3; 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 Reference proteome {ECO:0000313|Proteomes:UP000053244};
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 20..39
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 192..212
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 213..265
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 249..499
FT /note="Methyl-accepting transducer"
FT /evidence="ECO:0000259|PROSITE:PS50111"
FT REGION 278..297
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 278..295
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 528 AA; 55068 MW; AF3673CC2A94482A CRC64;
MTGNRGLGQW CRDRRVSTKV LAVAGVAIAG TVVTGALSVT GISDMASTRN AEIGMMAPYI
SNLNDAALSL KAAANDERGY LLEGDKKFAT EALGRQEKVT ASFDAARKLV TGDPAARVDE
IEAASNTWFV AIKSEFDLFQ AKPEAATTLA LETNRDLRKV YEGLLSAEIT SANQAMVAGQ
DFDHAVDRTR NLVIIALISA LLLGVSCALY VARLIIVPLR KVSGVLDQVA AGDLSGDPDV
HQRDELGHMA DSLRAATTSL RQTVTDLTAH SDSLAHEAGS LAATSKQSAG SAEEGAQQAA
TVAESAATMS FNIQTVAAGS EEMGASIREI SESATQAVHV ANRAVEVTAN TSAVMAKLGE
SSAEIGDVIK TITAIAEQTN LLALNATIES ARAGEMGKGF AVVASEVKEL SQETARATED
IGQRVAAIQA DTAGAVAAIE EISEIINRIN EFQTTIASAV EEQTVTTNEM SRNVTEAAEA
GARVADTITG VAASVQLTTV GVTEADRAAT QLAGMSTDLR RIVERFTL
//
