ID U5VPM7_9ACTN Unreviewed; 550 AA.
AC U5VPM7;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE SubName: Full=Putative methyl-accepting chemotaxis protein {ECO:0000313|EMBL:AGZ38918.1};
GN ORFNames=AFR_03145 {ECO:0000313|EMBL:AGZ38918.1};
OS Actinoplanes friuliensis DSM 7358.
OC Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC Micromonosporaceae; Actinoplanes.
OX NCBI_TaxID=1246995 {ECO:0000313|EMBL:AGZ38918.1, ECO:0000313|Proteomes:UP000017746};
RN [1] {ECO:0000313|EMBL:AGZ38918.1, ECO:0000313|Proteomes:UP000017746}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 7358 {ECO:0000313|EMBL:AGZ38918.1,
RC ECO:0000313|Proteomes:UP000017746};
RX PubMed=24637369; DOI=10.1016/j.jbiotec.2014.03.011;
RA Ruckert C., Szczepanowski R., Albersmeier A., Goesmann A., Fischer N.,
RA Steinkamper A., Puhler A., Biener R., Schwartz D., Kalinowski J.;
RT "Complete genome sequence of the actinobacterium Actinoplanes friuliensis
RT HAG 010964, producer of the lipopeptide antibiotic friulimycin.";
RL J. Biotechnol. 178:41-42(2014).
CC -!- SIMILARITY: Belongs to the methyl-accepting chemotaxis (MCP) protein
CC family. {ECO:0000256|ARBA:ARBA00029447}.
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DR EMBL; CP006272; AGZ38918.1; -; Genomic_DNA.
DR RefSeq; WP_023357861.1; NC_022657.1.
DR AlphaFoldDB; U5VPM7; -.
DR STRING; 1246995.AFR_03145; -.
DR KEGG; afs:AFR_03145; -.
DR PATRIC; fig|1246995.3.peg.633; -.
DR eggNOG; COG0840; Bacteria.
DR HOGENOM; CLU_000445_107_27_11; -.
DR OrthoDB; 1115140at2; -.
DR Proteomes; UP000017746; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0003824; F:catalytic activity; IEA:UniProt.
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; 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 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:UP000017746};
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 33..51
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 213..234
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 235..287
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 292..535
FT /note="Methyl-accepting transducer"
FT /evidence="ECO:0000259|PROSITE:PS50111"
SQ SEQUENCE 550 AA; 56863 MW; 2668719EC7FAE044 CRC64;
MPEAKMNEAV QVTVRRGPMA GLLADRSLAV KNVVAVAAMA VVAVVVGLLG LSRISEMSDD
LSIMKADHVD SLQQVAELRG GIADMFRGMV LYAVGTTDAE RKQGRSDVAA ADTKIDTALG
TYSTIAAKSA ARQQSITAFS DAMKNYRALR NTLLFQEPLA AGYTLPAADQ ISAEFSSVEG
EMNSAVADLQ KLEDTEADAL STEATNNFEN ARIFMITALI VGILLAGGIA LYVVRLIKQQ
LATVQTALGA VADNNLTIAA EVRSRDELGR MAVAVNRARE GLRTTITSLT AGAANLGNST
QQLTGVTARI GESAREAAAQ AGLVAGAAGD VSGSVQSVAA GSDEMGASIR EIAQNANDAA
QVASSAVGVA QSTNETVAKL GTSSAEIGDV VKVITAIAEQ TNLLALNATI EAARAGDAGK
GFAVVASEVK DLAQETARAT EDISRRVETI QTDTSSAVAA IGEISQIIQR INDYQVTIAS
AVEEQTATTA EMSRSISEAA GGSSTIAMNI NGVAHSAEQT SSTLVEADAA VSQLNRVADE
LRIVAERFRV
//
