ID A0A0F5R5F2_9BACL Unreviewed; 583 AA.
AC A0A0F5R5F2;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=Chemotaxis protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=VE23_15770 {ECO:0000313|EMBL:KKC48208.1};
OS Paenibacillus sp. D9.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=665792 {ECO:0000313|EMBL:KKC48208.1, ECO:0000313|Proteomes:UP000036611};
RN [1] {ECO:0000313|EMBL:KKC48208.1, ECO:0000313|Proteomes:UP000036611}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=D9 {ECO:0000313|EMBL:KKC48208.1,
RC ECO:0000313|Proteomes:UP000036611};
RA Sharma V., Lin J.;
RT "Genome sequence of surfactant producing, diesel degrading Paenibacillus
RT sp. D9, isolated from diesel contaminated soil.";
RL Submitted (MAR-2015) 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:KKC48208.1}.
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DR EMBL; JZEJ01000001; KKC48208.1; -; Genomic_DNA.
DR RefSeq; WP_049868496.1; NZ_JZEJ01000001.1.
DR AlphaFoldDB; A0A0F5R5F2; -.
DR PATRIC; fig|665792.3.peg.3530; -.
DR OrthoDB; 107771at2; -.
DR Proteomes; UP000036611; 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 Gene3D; 1.10.8.500; HAMP domain in histidine kinase; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000036611};
KW Transducer {ECO:0000256|ARBA:ARBA00023224, ECO:0000256|PROSITE-
KW ProRule:PRU00284}.
FT DOMAIN 203..256
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 275..511
FT /note="Methyl-accepting transducer"
FT /evidence="ECO:0000259|PROSITE:PS50111"
SQ SEQUENCE 583 AA; 62020 MW; 58678838FA1D57CD CRC64;
MKIRTNLLLG FSVVLALTLL VGAVSWNQLN SLHRTYQSLI QDRVGKILLI KDLKYRAASE
AKNVRGYLIT EQQASFDAYK ADRQSFATGM EKLKGSLKQE KSKELAGKLE RLEAEYAGIV
ATITGYKERG DTAGYIKLVE EQCIPMALKL SAAAEELESF QQSQLAASQA EAAAHVADVQ
KLLAAVVVLA LLLGAAAALL ISRRISRPVD AAARAARRIA EGDLTGDDLA PASIQELNVL
TLAVNGMKKQ LSQLLRTIDQ NARELAASSR QLAGASAQAA SESERISLSV RAIAESASGQ
RERMNESRTA MEESAISLQR VAEAASITAE SSEQALQQAD MGSRLMSETK GKMGEIRVVM
EGAAQNVENL VEQSGRIKEM AAFIHEVASQ TNLLSLNASI EAARAGEGGR GFAVVAQEVK
KLSEETKEAS ARISEFVLGI AEHADQAVES VKKGMEEVLR GSESIGNTEL AFRSVAYSMT
TVAQQTQEVS ASAEELSASM EQMLASSDEL LSLASTIAEH SGASAIGSRQ QMASMQDISG
SAESLQAMAA LLQEKLDAFH IEAEPSRAAV GTAQPLVPAI SAP
//