ID A0A168LLY2_9BACL Unreviewed; 562 AA.
AC A0A168LLY2;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Chemotaxis protein {ECO:0000313|EMBL:OAB43575.1};
GN ORFNames=PBAT_17890 {ECO:0000313|EMBL:OAB43575.1};
OS Paenibacillus antarcticus.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=253703 {ECO:0000313|EMBL:OAB43575.1, ECO:0000313|Proteomes:UP000077355};
RN [1] {ECO:0000313|EMBL:OAB43575.1, ECO:0000313|Proteomes:UP000077355}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CECT 5836 {ECO:0000313|EMBL:OAB43575.1,
RC ECO:0000313|Proteomes:UP000077355};
RA Shin S.-K., Yi H.;
RT "Draft genome sequence of Paenibacillus antarcticus CECT 5836.";
RL Submitted (MAR-2016) 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:OAB43575.1}.
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DR EMBL; LVJI01000027; OAB43575.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A168LLY2; -.
DR OrthoDB; 107771at2; -.
DR Proteomes; UP000077355; 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 CDD; cd11386; MCP_signal; 1.
DR Gene3D; 6.10.340.10; -; 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:UP000077355};
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 184..203
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 204..257
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 276..512
FT /note="Methyl-accepting transducer"
FT /evidence="ECO:0000259|PROSITE:PS50111"
SQ SEQUENCE 562 AA; 61150 MW; BA55363285D1E644 CRC64;
MTIGKKLIGS FLIIALLLGI TGVISSYYLN KIEGTYTDLI ERRAVILSNI LEAQVEVSKE
NSLLRGFMIT KDAEFLDKLK KSYDNATSLI SETEKLTQIN EFKEALQHLD KSNQAFKLKY
EQLIQMIQAN EHHIKTTDFF VNEVMPLGTL LDPIADKLAK DQLKSMNEES EKSSLIVKNA
IQNVAILSIL AFILAVFIGY VCSRMISKPI VAMSEVAERI ALGDLTIEDI KVKNNDEIGI
LAISFNQMTD NIRSLVRQIS ISSEQVASSS GELTASAEQT SQASEMITMS IQEVSTNAEM
QSRNVNESVQ SINEMSSGVQ QIASSAQMTS FLTIETAQKA VEGNHSIQLT AKQMDLIHHT
MNDLANAVTE MEEHSKEIEL IVEVISEIAA QTNLLSLNAA IEAARAGEQG RGFAVVAGEV
RKLAEQSSQS ATQISQLVTA IKSGTHNVVV STEAGVKEVS EGIQVVHTVG KLFEQIKRNI
DEVSNQVQEI SDASQQISAS TEQVVHSIGL ISDGSKTVAA ESQSLAASTE EQLASMEEIT
SSASSLSSMA EELQDLVAKF KV
//
