ID F7NH73_9FIRM Unreviewed; 584 AA.
AC F7NH73;
DT 21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT 21-SEP-2011, sequence version 1.
DT 24-JAN-2024, entry version 32.
DE SubName: Full=Methyl-accepting chemotaxis protein {ECO:0000313|EMBL:EGO64556.1};
GN ORFNames=ALO_07093 {ECO:0000313|EMBL:EGO64556.1};
OS Acetonema longum DSM 6540.
OC Bacteria; Bacillota; Negativicutes; Selenomonadales; Sporomusaceae;
OC Acetonema.
OX NCBI_TaxID=1009370 {ECO:0000313|EMBL:EGO64556.1, ECO:0000313|Proteomes:UP000003240};
RN [1] {ECO:0000313|EMBL:EGO64556.1, ECO:0000313|Proteomes:UP000003240}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 6540 {ECO:0000313|EMBL:EGO64556.1,
RC ECO:0000313|Proteomes:UP000003240};
RX PubMed=21673657; DOI=10.1038/emboj.2011.186;
RA Chen S., Beeby M., Murphy G.E., Leadbetter J.R., Hendrixson D.R.,
RA Briegel A., Li Z., Shi J., Tocheva E.I., Muller A., Dobro M.J.,
RA Jensen G.J.;
RT "Structural diversity of bacterial flagellar motors.";
RL EMBO J. 30:2972-2981(2011).
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:EGO64556.1}.
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DR EMBL; AFGF01000053; EGO64556.1; -; Genomic_DNA.
DR RefSeq; WP_004094104.1; NZ_AFGF01000053.1.
DR AlphaFoldDB; F7NH73; -.
DR STRING; 1009370.ALO_07093; -.
DR eggNOG; COG0840; Bacteria.
DR OrthoDB; 1672031at2; -.
DR Proteomes; UP000003240; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0007165; P:signal transduction; IEA:UniProtKB-KW.
DR CDD; cd06225; HAMP; 1.
DR CDD; cd18774; PDC2_HK_sensor; 1.
DR Gene3D; 1.10.287.950; Methyl-accepting chemotaxis protein; 1.
DR Gene3D; 3.30.450.20; PAS domain; 1.
DR InterPro; IPR003660; HAMP_dom.
DR InterPro; IPR004089; MCPsignal_dom.
DR PANTHER; PTHR32089:SF92; LYSOZYME-LIKE PROTEIN-RELATED; 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; 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:UP000003240};
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 21..50
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 209..227
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 228..280
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 299..570
FT /note="Methyl-accepting transducer"
FT /evidence="ECO:0000259|PROSITE:PS50111"
SQ SEQUENCE 584 AA; 63715 MW; B9FB999EA698CF55 CRC64;
MHRFMQFSAK IQSRLKQEHI AAAFASITAR VALFIIITCS VPLLLVGWYF TDQMIHSLTQ
AAIQRNNQVA DRIASDIDTF ILAQKNSVVL TSGKEEMRTT QPVVPGSLHT MIEHVLSQNP
GYAVTVMDKN RVPLYHQMDT TAVEARRTLD DSYFRVASEQ ESGFTEGIYR GQEYLVSFRP
IANTDWLVLS CYPKEVALQS AREMVRHSIY VTLLIVAVFV VLGLVAARKA LSPLKQLAAG
AEYVAEGHLS YRLATDHKDE FGTVAKAFNH MADRLGGIVG SVQESSRLVK NAADQVAASS
GELKVGSGQV VLALEGVTRQ IEQQTRETQT TEHLLEEMVR ISTAMSDSIK QVAAATDESV
TVATQGQTVI DQAMGQMRTL QQLVAKTESM MTVLDQSAHA IGQISLTISQ FSHQTNLLAL
NAAIEAARAG NAGRGFAVVA EEVRKLANES SGAVTQISEI VNKIQSETKE ALTSMRQSCE
YAGQGVAAAA DSGQAFSRIA ATVSHVQQEA GRIKIQTEKQ VELCHTAMQA MMSSNQLAMQ
TSAHGQEITS ISQEQAQIAI EMNHSIEKLR ELSSRLDSLV TQFK
//
