ID A0A0A0BLM0_9CELL Unreviewed; 549 AA.
AC A0A0A0BLM0;
DT 07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE SubName: Full=Chemotaxis protein {ECO:0000313|EMBL:KGM08861.1};
GN ORFNames=N869_09530 {ECO:0000313|EMBL:KGM08861.1};
OS Cellulomonas bogoriensis 69B4 = DSM 16987.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Cellulomonadaceae;
OC Cellulomonas.
OX NCBI_TaxID=1386082 {ECO:0000313|EMBL:KGM08861.1, ECO:0000313|Proteomes:UP000054314};
RN [1] {ECO:0000313|EMBL:KGM08861.1, ECO:0000313|Proteomes:UP000054314}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=69B4 {ECO:0000313|EMBL:KGM08861.1,
RC ECO:0000313|Proteomes:UP000054314};
RA Chen F., Li Y., Wang G.;
RT "Genome sequencing of Cellulomonas bogoriensis 69B4.";
RL Submitted (AUG-2013) 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:KGM08861.1}.
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DR EMBL; AXCZ01000241; KGM08861.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0A0BLM0; -.
DR OrthoDB; 3378718at2; -.
DR Proteomes; UP000054314; 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; IPR004090; Chemotax_Me-accpt_rcpt.
DR InterPro; IPR003660; HAMP_dom.
DR InterPro; IPR024478; HlyB_4HB_MCP.
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; PF12729; 4HB_MCP_1; 1.
DR Pfam; PF00672; HAMP; 1.
DR Pfam; PF00015; MCPsignal; 1.
DR PRINTS; PR00260; CHEMTRNSDUCR.
DR SMART; SM00304; HAMP; 2.
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:UP000054314};
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 211..233
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 234..286
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 291..520
FT /note="Methyl-accepting transducer"
FT /evidence="ECO:0000259|PROSITE:PS50111"
SQ SEQUENCE 549 AA; 56339 MW; B9DF5A797B93B51F CRC64;
MGRMARAASG RRGLGRPIGS VRTKILLSLA CVSLVAVAVA VVGLARLHTM EQRVTTMRDV
NVEQATELGD VRAGFMEMYY ELVGVAGLSS MMPPDTPEFV AAQAQGRDAV IAADARIAEA
LDAYRAEAGE SPERAAVLAE FDEHLDAYMT FRDVWFFGAT PPAGWELPTE SDQITALNTN
LSETLDALAA IEGAEADAAA DAAGQALRTS LVNVVLSLTV GLSVGVVIAV AVARGVSGRL
GQVAEVVDAL GDGDLTRTVH VSGSDEVARM AAAVTSATER LRPMLGTLAG TSEEVAGHAA
TIACTTASTG DRADEASARA GDVAAAADQV SGNVQSVATG AQQMSSSIRE IARNATAASE
VAARAVVAAR STNETVGRLG DSSAEIGTVV RTITSIAEQT NLLALNATIE AARAGEAGKG
FAVVAGEVKE LAQATARATE DIAHRIDVIQ GDTDSAMGAI GEITAIVQQI DEYQSTIASA
VEEQNATTDE MSRGVDQAAD GTGEIAAGIS GVARSTSDAA ESLRAGREAA AELSGLAVQM
KELVHRFRF
//
