ID A0A158I1C4_9BURK Unreviewed; 518 AA.
AC A0A158I1C4;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=Methyl-accepting chemotaxis sensory transducer {ECO:0000313|EMBL:SAL50378.1};
GN ORFNames=AWB69_05107 {ECO:0000313|EMBL:SAL50378.1};
OS Caballeronia udeis.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Caballeronia.
OX NCBI_TaxID=1232866 {ECO:0000313|EMBL:SAL50378.1, ECO:0000313|Proteomes:UP000054683};
RN [1] {ECO:0000313|EMBL:SAL50378.1, ECO:0000313|Proteomes:UP000054683}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LMG 27134 {ECO:0000313|EMBL:SAL50378.1};
RA Oliw E.H.;
RL Submitted (JAN-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000256|ARBA:ARBA00004429}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004429}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the methyl-accepting chemotaxis (MCP) protein
CC family. {ECO:0000256|ARBA:ARBA00029447}.
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DR EMBL; FCOK02000038; SAL50378.1; -; Genomic_DNA.
DR RefSeq; WP_075643981.1; NZ_FCOK02000038.1.
DR AlphaFoldDB; A0A158I1C4; -.
DR OrthoDB; 9806477at2; -.
DR Proteomes; UP000054683; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004888; F:transmembrane signaling receptor activity; IEA:InterPro.
DR GO; GO:0006935; P:chemotaxis; 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; 1.20.120.30; Aspartate receptor, ligand-binding domain; 1.
DR Gene3D; 1.10.287.950; Methyl-accepting chemotaxis protein; 1.
DR InterPro; IPR035440; 4HB_MCP_dom_sf.
DR InterPro; IPR004090; Chemotax_Me-accpt_rcpt.
DR InterPro; IPR003660; HAMP_dom.
DR InterPro; IPR004089; MCPsignal_dom.
DR InterPro; IPR003122; Tar_rcpt_lig-bd.
DR PANTHER; PTHR43531:SF14; METHYL-ACCEPTING CHEMOTAXIS PROTEIN I-RELATED; 1.
DR PANTHER; PTHR43531; PROTEIN ICFG; 1.
DR Pfam; PF00672; HAMP; 1.
DR Pfam; PF00015; MCPsignal; 1.
DR Pfam; PF02203; TarH; 1.
DR PRINTS; PR00260; CHEMTRNSDUCR.
DR SMART; SM00304; HAMP; 1.
DR SMART; SM00283; MA; 1.
DR SUPFAM; SSF47170; Aspartate receptor, ligand-binding domain; 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 Chemotaxis {ECO:0000256|ARBA:ARBA00022500};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Methylation {ECO:0000256|ARBA:ARBA00022481};
KW Transducer {ECO:0000256|PROSITE-ProRule:PRU00284};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..33
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 190..213
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 215..267
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 272..501
FT /note="Methyl-accepting transducer"
FT /evidence="ECO:0000259|PROSITE:PS50111"
SQ SEQUENCE 518 AA; 54355 MW; 045C8520E06BD2F7 CRC64;
MLRNLSIKTG LTLATSVFVL LVLVVGTCAF VSLGRANHAL SGMYEHDLAG STALTRSSEL
LLRCRSAKNR YESLIADNKA DDAAKQLATA HEYCSESQKQ WDAFAALPVP GDAQGLITDA
AAKHAAMMQK GIMPEFDALE AKDFDAYKRI QMQFSSPLYN QFDQLSQPLL GYVSSRAQQR
FEGAQTTADI VNTVLVACAL LALVIGITVR VALTRLVVKP ITAMAADFER IAGGDLHTPI
IVESDNEMGQ LQGALRRMQT ELATTVRHIR HSAESITVAA GEIASGNIDL SARTEQQAAS
LQETAASMEQ ISGTVQRNAD NASQATTLAA NASTIASHGS AVVNNVISTM ADISQSSAKI
ADIITIIEGI AFQTNILALN AAVEAARAGE EGRGFAVVAG EVRSLAQRSS SAAKEIKGLI
DTSVERVNAG SGLVGEAGTT MTQITQAVQR VTSIMGEISA ASGEQSRGIS QVATAVTQMD
GVTQRNAALV EEAAAAAQSL EDQAKSLKDA LAIFSVSA
//