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Database: UniProt
Entry: A0A1I0KGH7_9BACL
LinkDB: A0A1I0KGH7_9BACL
Original site: A0A1I0KGH7_9BACL 
ID   A0A1I0KGH7_9BACL        Unreviewed;       523 AA.
AC   A0A1I0KGH7;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   SubName: Full=Methyl-accepting chemotaxis protein {ECO:0000313|EMBL:SEU23539.1};
GN   ORFNames=SAMN03159358_4208 {ECO:0000313|EMBL:SEU23539.1};
OS   Paenibacillus sp. NFR01.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX   NCBI_TaxID=1566279 {ECO:0000313|EMBL:SEU23539.1, ECO:0000313|Proteomes:UP000198735};
RN   [1] {ECO:0000313|EMBL:SEU23539.1, ECO:0000313|Proteomes:UP000198735}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NFR01 {ECO:0000313|EMBL:SEU23539.1,
RC   ECO:0000313|Proteomes:UP000198735};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the methyl-accepting chemotaxis (MCP) protein
CC       family. {ECO:0000256|ARBA:ARBA00029447}.
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DR   EMBL; FOIK01000005; SEU23539.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1I0KGH7; -.
DR   STRING; 1566279.SAMN03159358_4208; -.
DR   Proteomes; UP000198735; Unassembled WGS sequence.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
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:SF92; LYSOZYME-LIKE PROTEIN-RELATED; 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   Cell membrane {ECO:0000256|ARBA:ARBA00022475};
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}; Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        188..211
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          208..260
FT                   /note="HAMP"
FT                   /evidence="ECO:0000259|PROSITE:PS50885"
FT   DOMAIN          265..508
FT                   /note="Methyl-accepting transducer"
FT                   /evidence="ECO:0000259|PROSITE:PS50111"
SQ   SEQUENCE   523 AA;  56091 MW;  886C12A7A400E50B CRC64;
     MKLNIRKKLL GSFLVVVALL VFISILSVNK MGQMNSSSEK MRDIALPGVV NMEGIRTNLL
     KLRGDLMKLI LETQESEMQK IEQAIKEDQA KITENIKAYE ELKLTAEQKA SLEVIKENVK
     NYNAIVPQTI EYGLNNDIQN GYKMLLQSLP DLQSALDTAN QAAISAIDGA NTNVDTILRS
     YKSGSTTILI FAAVAVGIAV ALALFISQSI VKSASKLVRL MSLISEGDLR ETVTIHSRDE
     FGKLADAANL TILSLKKLIG QTMESAQSVA ASSQEISATA EEIANGSQSQ AQAAQNINQL
     TQDLVRGIDE VARNAEQVSE LSIQARQGAE EGRKAVRESS LGMGKLSEKI GILEQDSHKI
     GEIIEVIDEI AEQTNLLALN AAIEAARAGE QGRGFAVVAD EVRKLAERSG EATKQIAHII
     RGMQQNTILS VEAVSEASIL SDKTEVLIEG IVSRVNETTQ QITSIAAACE EQAAQSSEVL
     FSIEAVAAGS QESAAAAEET AASTQILAKL ADELNNSVSA FKL
//
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