ID A0A0B2JWG3_9FIRM Unreviewed; 571 AA.
AC A0A0B2JWG3;
DT 04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT 04-MAR-2015, sequence version 1.
DT 24-JAN-2024, entry version 31.
DE RecName: Full=Chemotaxis protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=NZ47_07580 {ECO:0000313|EMBL:KHM51949.1};
OS Anaerovibrio lipolyticus.
OC Bacteria; Bacillota; Negativicutes; Selenomonadales; Selenomonadaceae;
OC Anaerovibrio.
OX NCBI_TaxID=82374 {ECO:0000313|EMBL:KHM51949.1, ECO:0000313|Proteomes:UP000030993};
RN [1] {ECO:0000313|EMBL:KHM51949.1, ECO:0000313|Proteomes:UP000030993}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=5S {ECO:0000313|EMBL:KHM51949.1,
RC ECO:0000313|Proteomes:UP000030993};
RX PubMed=23950883;
RA Prive F., Kaderbhai N.N., Girdwood S., Worgan H.J., Pinloche E.,
RA Scollan N.D., Huws S.A., Newbold C.J.;
RT "Identification and characterization of three novel lipases belonging to
RT families II and V from Anaerovibrio lipolyticus 5ST.";
RL PLoS ONE 8:E69076-E69076(2013).
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:KHM51949.1}.
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DR EMBL; JSCE01000157; KHM51949.1; -; Genomic_DNA.
DR RefSeq; WP_039208677.1; NZ_JSCE01000157.1.
DR AlphaFoldDB; A0A0B2JWG3; -.
DR STRING; 82374.NZ47_07580; -.
DR eggNOG; COG0840; Bacteria.
DR Proteomes; UP000030993; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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; 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 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 Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000030993};
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 13..32
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 192..212
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 213..266
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 285..521
FT /note="Methyl-accepting transducer"
FT /evidence="ECO:0000259|PROSITE:PS50111"
SQ SEQUENCE 571 AA; 61858 MW; 631354B8E2E25705 CRC64;
MNFFYNLKMV YKILTLVVIA AIGMALIGYR GYSTISESRD SLEVIYQKNM QQLYCIGEIK
YMLRDMQSRG ALSLSAKDQK RIDDLRNDQK EIRENFESNW KLYEQATSGT EAEKANAAIL
EKWKVFGAAI DQVIALAEAN NKDEGATYLS KNAGDATKQL RLLLEAQQKQ AQENSQALFE
KMESDATSAS RMMVLFSVAA LIALFAFSML IIKAITGPLN RMMETCRHMG DGDFRITPRT
ITTTDEIGEL ADTVCIMREN LNKLMRQTSS SAEQIAAAGE ELTASAQQSA QASTQVAQSV
TDAAGAVQIQ QGAIESSTQA VSNINDSVSA IDNQSNNVAS RADSAAKSAA QGLKSIEETI
KQIRNGAVGV QDSSEIVDRL GESSQEIGTI VETISGIAEQ TNLLALNAAI EAARAGEHGR
GFAVVAEEVR KLAEQSGEAA QKITQLITGI QQETQQAVTS MQKGRATVDA GAESVANLRQ
NFIEIESLVN EVTQEVKQMS QAVHSATSDT ENITTQVENI DKQGRAVSDE MQTVSAATEE
QSASASEIAT ASESLSKLAE DLQHSLHQFK F
//
