ID A0A2T0R598_9ACTN Unreviewed; 539 AA.
AC A0A2T0R598;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 14.
DE SubName: Full=Methyl-accepting chemotaxis protein {ECO:0000313|EMBL:PRY15929.1};
GN ORFNames=CLV37_104142 {ECO:0000313|EMBL:PRY15929.1};
OS Kineococcus rhizosphaerae.
OC Bacteria; Actinomycetota; Actinomycetes; Kineosporiales; Kineosporiaceae;
OC Kineococcus.
OX NCBI_TaxID=559628 {ECO:0000313|EMBL:PRY15929.1, ECO:0000313|Proteomes:UP000238083};
RN [1] {ECO:0000313|EMBL:PRY15929.1, ECO:0000313|Proteomes:UP000238083}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 19711 {ECO:0000313|EMBL:PRY15929.1,
RC ECO:0000313|Proteomes:UP000238083};
RA Goeker M.;
RT "Genomic Encyclopedia of Archaeal and Bacterial Type Strains, Phase II
RT (KMG-II): from individual species to whole genera.";
RL Submitted (MAR-2018) 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:PRY15929.1}.
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DR EMBL; PVZF01000004; PRY15929.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2T0R598; -.
DR OrthoDB; 8667074at2; -.
DR Proteomes; UP000238083; 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; 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 Coiled coil {ECO:0000256|SAM:Coils}; Membrane {ECO:0000256|SAM:Phobius};
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 25..47
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 203..223
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 224..276
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 281..510
FT /note="Methyl-accepting transducer"
FT /evidence="ECO:0000259|PROSITE:PS50111"
FT COILED 171..198
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 539 AA; 54561 MW; AAF14F9978E4A8DC CRC64;
MSSALPVSTS RTTRVFADRS VRTKVLSALG ALGLVTIGVS AGSLVALDEG AQRADATYQD
TVLGLTALGR VHQEELKTRM LVAQHAATPD AEGKAKVAQK IKDSDAELDT WAAKYSASPL
ADAADWKSFT DTWAQWRQAR DTQLLPLSEA GDQAGWAKAN ADVAQPLVSS AADALDAVEG
AENKVAEASA AASRTTAKDS RNLILAALAL GLGLSGALGL AVVRSIVRPL HEVSASLEAM
AEGDLTVAAR VESRDEVGQM AASLEKARAS VRGTVSAIAS SSQSLLLASD QLTADSERIG
GTAGQTASAA ASAADTAATV SASVSTVAMG ADEMQAAIRD IANGASEATA VAARADELAG
RAGETVARLG VSSAQIGDVV KAITAIAEQT NLLALNATIE AARAGEAGKG FAVVAGEVKE
LSAQTARATE DIAARVGSIQ TDTAEAVRAI ESIAEVIGEI GNHQTTIASA VEEQSATTAE
MSRSVGEAAA GSERIADSIR GITGSAATTA EVVAGSRTAA DDLARLSGEL SFLVTRFKV
//
