ID A0A120IHF6_9BURK Unreviewed; 509 AA.
AC A0A120IHF6;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=Chemotaxis protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=VN23_04105 {ECO:0000313|EMBL:AMC33839.1};
OS Janthinobacterium sp. B9-8.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Oxalobacteraceae; Janthinobacterium.
OX NCBI_TaxID=1236179 {ECO:0000313|EMBL:AMC33839.1, ECO:0000313|Proteomes:UP000069577};
RN [1] {ECO:0000313|EMBL:AMC33839.1, ECO:0000313|Proteomes:UP000069577}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B9-8 {ECO:0000313|EMBL:AMC33839.1,
RC ECO:0000313|Proteomes:UP000069577};
RA Xu X., Jin W., Wu Q., Jiang L., Huang H.;
RT "The whole genome sequence of Janthinbacterium sp. B9-8, a bacterium
RT isolated from low temperature sewage.";
RL Submitted (JAN-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; CP014222; AMC33839.1; -; Genomic_DNA.
DR RefSeq; WP_046349803.1; NZ_CP014222.1.
DR AlphaFoldDB; A0A120IHF6; -.
DR STRING; 1236179.VN23_04105; -.
DR KEGG; jab:VN23_04105; -.
DR OrthoDB; 8576332at2; -.
DR Proteomes; UP000069577; Chromosome.
DR GO; GO:0016020; C: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; 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:SF112; HEME-BASED AEROTACTIC TRANSDUCER HEMAT; 1.
DR PANTHER; PTHR32089; METHYL-ACCEPTING CHEMOTAXIS PROTEIN MCPB; 1.
DR Pfam; PF12729; 4HB_MCP_1; 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 Coiled coil {ECO:0000256|SAM:Coils}; Membrane {ECO:0000256|SAM:Phobius};
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 12..31
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 188..207
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..482
FT /note="Methyl-accepting transducer"
FT /evidence="ECO:0000259|PROSITE:PS50111"
FT COILED 156..183
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 509 AA; 56119 MW; 3AEE2B597ACEF315 CRC64;
MKISIKYKVM LPALLSIGLL LGIATVAYLW VGRQVQATEL LYDTNYKKSH ALNRIANDAY
MIRGDVYQLL ASIRSNNDQA RSRVLGKALI SKLDDAIEKI GQVGVDELGA DRVSQLKNAL
YKYRMLLIDA FDMFGNDDNL AGMIVLSADP SFVAFNVLLR QELELQNKNM AEQQEKNTQH
REQSSRRFIL LSVAALCFSL LSAWFLGGRL SAMIIHFSEN IRHCAQGDLS HEMIKKSDDE
IGAAIESFEY MRKNLIGLIA AIQDQADRVG DLVAQINLSC DETLQQSHHQ SQMMSNNFGT
LEALSGSISL VGNIGNDAAH KFNEMQQRTL GILNTSGKQL DRSLEIKKIV FLIEKIAEKT
NLLALNAAIE AARAGEKGRG FGVVAAEVRR LAEQTAVATL EIGKLIHDDG ISADAAEANN
EAGKGQLKIE QIIQQINHEA DQFKADLNEL NLAMDQQIKS VQSVSETMAL FLQQTRSTQN
ITTLTAEHAK ALKASAEPLL NAIGRFSVH
//
