ID A0A1H3NX08_9ACTN Unreviewed; 513 AA.
AC A0A1H3NX08;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE SubName: Full=Methyl-accepting chemotaxis sensory transducer with Cache sensor {ECO:0000313|EMBL:SDY93368.1};
GN ORFNames=SAMN05444365_104207 {ECO:0000313|EMBL:SDY93368.1};
OS Micromonospora pattaloongensis.
OC Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC Micromonosporaceae; Micromonospora.
OX NCBI_TaxID=405436 {ECO:0000313|EMBL:SDY93368.1, ECO:0000313|Proteomes:UP000242415};
RN [1] {ECO:0000313|Proteomes:UP000242415}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 45245 {ECO:0000313|Proteomes:UP000242415};
RA Varghese N., Submissions S.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {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; FNPH01000004; SDY93368.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H3NX08; -.
DR STRING; 405436.SAMN05444365_104207; -.
DR Proteomes; UP000242415; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma 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; 6.10.340.10; -; 1.
DR Gene3D; 1.10.287.950; Methyl-accepting chemotaxis protein; 1.
DR Gene3D; 3.30.450.20; PAS domain; 1.
DR InterPro; IPR004090; Chemotax_Me-accpt_rcpt.
DR InterPro; IPR003660; HAMP_dom.
DR InterPro; IPR004089; MCPsignal_dom.
DR InterPro; IPR033480; sCache_2.
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 PRINTS; PR00260; CHEMTRNSDUCR.
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.
PE 3: Inferred from homology;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Reference proteome {ECO:0000313|Proteomes:UP000242415};
KW Transducer {ECO:0000256|ARBA:ARBA00023224, ECO:0000256|PROSITE-
KW ProRule:PRU00284}; Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT DOMAIN 213..265
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 305..500
FT /note="Methyl-accepting transducer"
FT /evidence="ECO:0000259|PROSITE:PS50111"
FT COILED 256..283
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 513 AA; 53950 MW; DE1DDF4AFA7C57E2 CRC64;
MRRLLNVGIF VKLAVVAGVA IAGLLAMGAA RLAEVAPMEL ESRKAKVRAL VESATSVIAG
YHAATQNGTM TTEQAQRAAL TALKAMRYGA DDYFFVNDMH PVMVMHPMKP ELDGKDLSTN
ADPNGKLLFV EFVKVVRAEG AGFVDYQWPK PGHDAPVDKL TYVAGFEPWG WVVGTGIYID
DMHAAIAAHE RDVMVQTGAI MLGVAVVLVL VGLSITRPVR SLTLATRRLA DGQLDVALPS
PGRGELGRMS AALGVLRDGL AERQALAEER DRMRAQAEAE KRRAADDVAD RLEATVDTVA
GRLKEAVEAM QRGAAELGDT TGQLVGTVRE ISHLAGESSD VAGRAAAEAT DASGTVNGLT
TAADTIGGVV EVIRKVAAQT NLLALNATIE AARAGEIGKG FAVVAGEVKE LAQQSSRATD
EIAREIESIQ STSQEAARVM DRMADTVERL GSSTREVAAA IAGGDSEGAS VRGSAEATGQ
VAHRIQQLSG ELSAEADRLR GDFGVLLSQL RQG
//
