ID H6LG12_ACEWD Unreviewed; 573 AA.
AC H6LG12;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 27-MAR-2024, entry version 59.
DE SubName: Full=Putative methyl-accepting chemotaxis transducer protein {ECO:0000313|EMBL:AFA48300.1};
GN OrderedLocusNames=Awo_c15180 {ECO:0000313|EMBL:AFA48300.1};
OS Acetobacterium woodii (strain ATCC 29683 / DSM 1030 / JCM 2381 / KCTC 1655
OS / WB1).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Eubacteriaceae;
OC Acetobacterium.
OX NCBI_TaxID=931626 {ECO:0000313|EMBL:AFA48300.1, ECO:0000313|Proteomes:UP000007177};
RN [1] {ECO:0000313|Proteomes:UP000007177}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29683 / DSM 1030 / JCM 2381 / KCTC 1655 / WB1
RC {ECO:0000313|Proteomes:UP000007177};
RA Poehlein A., Schmidt S., Kaster A.-K., Goenrich M., Vollmers J.,
RA Thuermer A., Gottschalk G., Thauer R.K., Daniel R., Mueller V.;
RT "Complete genome sequence of Acetobacterium woodii.";
RL Submitted (JUL-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:AFA48300.1, ECO:0000313|Proteomes:UP000007177}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29683 / DSM 1030 / JCM 2381 / KCTC 1655 / WB1
RC {ECO:0000313|Proteomes:UP000007177};
RX PubMed=22479398; DOI=10.1371/journal.pone.0033439;
RA Poehlein A., Schmidt S., Kaster A.K., Goenrich M., Vollmers J., Thurmer A.,
RA Bertsch J., Schuchmann K., Voigt B., Hecker M., Daniel R., Thauer R.K.,
RA Gottschalk G., Muller V.;
RT "An ancient pathway combining carbon dioxide fixation with the generation
RT and utilization of a sodium ion gradient for ATP synthesis.";
RL PLoS ONE 7:E33439-E33439(2012).
CC -!- SIMILARITY: Belongs to the methyl-accepting chemotaxis (MCP) protein
CC family. {ECO:0000256|ARBA:ARBA00029447}.
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DR EMBL; CP002987; AFA48300.1; -; Genomic_DNA.
DR RefSeq; WP_014355903.1; NC_016894.1.
DR AlphaFoldDB; H6LG12; -.
DR STRING; 931626.Awo_c15180; -.
DR KEGG; awo:Awo_c15180; -.
DR eggNOG; COG0840; Bacteria.
DR eggNOG; COG4192; Bacteria.
DR HOGENOM; CLU_000445_107_16_9; -.
DR OrthoDB; 9814363at2; -.
DR Proteomes; UP000007177; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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 CDD; cd19411; MCP2201-like_sensor; 1.
DR CDD; cd11386; MCP_signal; 1.
DR Gene3D; 6.10.340.10; -; 1.
DR Gene3D; 1.10.287.950; Methyl-accepting chemotaxis protein; 1.
DR InterPro; IPR004090; Chemotax_Me-accpt_rcpt.
DR InterPro; IPR003660; HAMP_dom.
DR InterPro; IPR024478; HlyB_4HB_MCP.
DR InterPro; IPR004089; MCPsignal_dom.
DR InterPro; IPR047347; YvaQ-like_sensor.
DR PANTHER; PTHR43531:SF11; METHYL-ACCEPTING CHEMOTAXIS PROTEIN 3; 1.
DR PANTHER; PTHR43531; PROTEIN ICFG; 1.
DR Pfam; PF12729; 4HB_MCP_1; 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:UP000007177};
KW Transducer {ECO:0000256|PROSITE-ProRule:PRU00284};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 191..211
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 212..264
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 269..498
FT /note="Methyl-accepting transducer"
FT /evidence="ECO:0000259|PROSITE:PS50111"
FT REGION 521..573
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 532..546
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 573 AA; 62560 MW; 583DEC6A375E3758 CRC64;
MKFFENLKIK QKLLTCFILF AVVTAVVGGF GIYTMNGINN QSKNMYYDNL LPSQKLANIQ
ATLGEIRANQ LLALYERNPG TLQTRLDVIN AESEENNTLL KEYETNIRNE EDRALFATLT
ESVATYRDIR NQNIDLLKNG KYDQALAEIN QVTQAREAVD QDLEALITYN TTLAEEILNQ
NTASFQTQST IMIIFIMIGI ALAVGLGLMV ANMISKPLQR MVEAAEAIAD GNLNVMIKID
GRDEVGELGL AFEKMTGHIN EIMTNIDSAA EQVAAGSKQI ADSSIGLSQG ATEQASSIEQ
LTASIEEISS QTRINADNAN EANELAEITK ENAELGNSEM KLMLQSMEEI NESSSNISKI
IKVIDEIAFQ TNILALNAAV EAARARQHGK GFAVVAEEVR NLAARSADAA KETTRMIEGS
IKKVDDGRKI ASKTADALDK IVGNVAKVSD IVGNIASASN EQAIGISQIN QGIMQVSEVV
QVNSATSEES ASASEELSSQ AELLREQAAW FQLKNIGNFN HNARENQSSD RFDPPRGNQQ
QSRRGKRGNQ TEGKAPIPKV TRIALSDNEF GKY
//
