ID A0A1I0KR13_9BACL Unreviewed; 725 AA.
AC A0A1I0KR13;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE SubName: Full=Methyl-accepting chemotaxis protein {ECO:0000313|EMBL:SEU27353.1};
GN ORFNames=SAMN03159358_4559 {ECO:0000313|EMBL:SEU27353.1};
OS Paenibacillus sp. NFR01.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=1566279 {ECO:0000313|EMBL:SEU27353.1, ECO:0000313|Proteomes:UP000198735};
RN [1] {ECO:0000313|EMBL:SEU27353.1, ECO:0000313|Proteomes:UP000198735}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NFR01 {ECO:0000313|EMBL:SEU27353.1,
RC ECO:0000313|Proteomes:UP000198735};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the methyl-accepting chemotaxis (MCP) protein
CC family. {ECO:0000256|ARBA:ARBA00029447}.
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DR EMBL; FOIK01000007; SEU27353.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I0KR13; -.
DR STRING; 1566279.SAMN03159358_4559; -.
DR Proteomes; UP000198735; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR GO; GO:0006935; P:chemotaxis; IEA:UniProtKB-KW.
DR GO; GO:0007165; P:signal transduction; IEA:UniProtKB-KW.
DR CDD; cd06225; HAMP; 1.
DR CDD; cd12913; PDC1_MCP_like; 1.
DR CDD; cd12912; PDC2_MCP_like; 1.
DR Gene3D; 1.10.8.500; HAMP domain in histidine kinase; 1.
DR Gene3D; 1.10.287.950; Methyl-accepting chemotaxis protein; 1.
DR Gene3D; 3.30.450.20; PAS domain; 2.
DR InterPro; IPR033479; dCache_1.
DR InterPro; IPR003660; HAMP_dom.
DR InterPro; IPR004089; MCPsignal_dom.
DR InterPro; IPR029151; Sensor-like_sf.
DR PANTHER; PTHR32089:SF92; LYSOZYME-LIKE PROTEIN-RELATED; 1.
DR PANTHER; PTHR32089; METHYL-ACCEPTING CHEMOTAXIS PROTEIN MCPB; 1.
DR Pfam; PF02743; dCache_1; 1.
DR Pfam; PF00672; HAMP; 1.
DR Pfam; PF00015; MCPsignal; 1.
DR SMART; SM00304; HAMP; 2.
DR SMART; SM00283; MA; 1.
DR SUPFAM; SSF58104; Methyl-accepting chemotaxis protein (MCP) signaling domain; 1.
DR SUPFAM; SSF103190; Sensory domain-like; 1.
DR PROSITE; PS50111; CHEMOTAXIS_TRANSDUC_2; 1.
DR PROSITE; PS50885; HAMP; 1.
PE 3: Inferred from homology;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Chemotaxis {ECO:0000256|ARBA:ARBA00022500};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000198735};
KW Transducer {ECO:0000256|ARBA:ARBA00023224, ECO:0000256|PROSITE-
KW ProRule:PRU00284};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 58..79
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 345..365
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 367..419
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 438..696
FT /note="Methyl-accepting transducer"
FT /evidence="ECO:0000259|PROSITE:PS50111"
FT REGION 1..35
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 725 AA; 78273 MW; E7A4550B59FCAAB9 CRC64;
MPLWKRKNEK AVSGPQPELM ESTTHPLNGE AENGKPAVPK LPKAMLSRFA RMGIRGKLFV
TVLMSVGVIF VAVAVIIYIN AKNIIVDDLN SSLTYEKTGI SAKIDQLLQP ASDSVGLLNA
NAYVRDFLTR VPSADALKET EGYPEFIQTL KLIKNGNKSL LNVYVGVASI NRLVTQDEFD
PPADYNLKER GWYATTAKNK RLTVTDPYID AATGKMVVSV SAPILNQTGQ LIGVAGADIA
TDQIIAALSS FQYNDSGYAL LIDKSGTFIY HPNTDNILLK QIRLLGKDWE KVGDRMLQWG
SDVFKTTVDG VPSYISYAPV VDNQWSVALV VPQKAAEQEL QSFEVIFVIS IAASLVLMAL
LLYFVSNSIL KPIPRLTAAF KQAMAGDLSA RAKVRDKGEI GLLADGFNDM LSTQQALISE
IKRTSESISG AVDNTEKNVF SLDVSINDIS AITEELSAGL QQTAASMEEM NASTTEFEHA
VGSIAHQAEQ GAVAAREINE RAERLKTASH LARERADAAY REGQRDLRSA IKQSRTIGQI
KVLSDAILEI ASQTNLLSLN ASIEAARAGE AGRGFAVVAE EIRKLAEGAR DTVSEIQDVT
ESVVRAVAGL VGSAEGMLQF MDSHVQSDYN TMQTTGEQYS EDARYIEKLM TGFSETSGQL
LVSIQSMLTA IGETSIATGE GAEGASSIAA QAEQIIGKSG GIVTEMEEIR HSASELLKAV
SRFKA
//