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Database: UniProt
Entry: A0A158JTF0_9BURK
LinkDB: A0A158JTF0_9BURK
Original site: A0A158JTF0_9BURK 
ID   A0A158JTF0_9BURK        Unreviewed;       516 AA.
AC   A0A158JTF0;
DT   27-SEP-2017, integrated into UniProtKB/TrEMBL.
DT   27-SEP-2017, sequence version 1.
DT   27-MAR-2024, entry version 16.
DE   SubName: Full=Methyl-accepting chemotaxis sensory transducer {ECO:0000313|EMBL:SAL72087.1};
GN   ORFNames=AWB66_04625 {ECO:0000313|EMBL:SAL72087.1};
OS   Caballeronia telluris.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Caballeronia.
OX   NCBI_TaxID=326475 {ECO:0000313|EMBL:SAL72087.1, ECO:0000313|Proteomes:UP000054717};
RN   [1] {ECO:0000313|EMBL:SAL72087.1, ECO:0000313|Proteomes:UP000054717}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LMG 22936 {ECO:0000313|EMBL:SAL72087.1};
RA   Oliw E.H.;
RL   Submitted (JAN-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {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; FCNZ02000020; SAL72087.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A158JTF0; -.
DR   STRING; 326475.AWB66_04625; -.
DR   Proteomes; UP000054717; Unassembled WGS sequence.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR   GO; GO:0007165; P:signal transduction; IEA:UniProtKB-KW.
DR   CDD; cd11386; MCP_signal; 1.
DR   Gene3D; 1.10.287.950; Methyl-accepting chemotaxis protein; 1.
DR   Gene3D; 3.30.450.20; PAS domain; 1.
DR   InterPro; IPR003660; HAMP_dom.
DR   InterPro; IPR004089; MCPsignal_dom.
DR   InterPro; IPR033480; sCache_2.
DR   PANTHER; PTHR43531:SF14; METHYL-ACCEPTING CHEMOTAXIS PROTEIN I-RELATED; 1.
DR   PANTHER; PTHR43531; PROTEIN ICFG; 1.
DR   Pfam; PF00015; MCPsignal; 1.
DR   Pfam; PF17200; sCache_2; 1.
DR   SMART; SM01049; Cache_2; 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   Coiled coil {ECO:0000256|SAM:Coils};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054717};
KW   Transducer {ECO:0000256|PROSITE-ProRule:PRU00284};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        12..30
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        190..209
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          214..265
FT                   /note="HAMP"
FT                   /evidence="ECO:0000259|PROSITE:PS50885"
FT   DOMAIN          270..499
FT                   /note="Methyl-accepting transducer"
FT                   /evidence="ECO:0000259|PROSITE:PS50111"
FT   COILED          470..508
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   516 AA;  55225 MW;  6C75615736D360E3 CRC64;
     MNKLTLNQKL SSMIAVLWIG LIAIGIIGAW QNRASMIEDR RDQLTTLIGQ AHSVASHFQT
     LAANRAITED EAKKKALEVI ASMRYGADGY ISINDSHPTI VMHPIKSAMN GQDVSNFADP
     QGTKLFVEIV KAGNHEKGGF VNYLWPKPGY DQPVAKMSYS QRFAPWDWYL VTGMYMDDVQ
     AAFYASALRW LGITALLGVL ATVAMLLVLK SIKRNLGGDL ELAVSAAHRI ARGDLTTPVH
     VHEKDTSSLL YALSSMQSGL VETVSRVRNG TENINVGASE IAAGNTDLSQ RTEQQAAALV
     ETASSMDEMT ANVKQNADSA TQAARLAEQA ADVATRGSSV VADVIHTMTR ITDSSKQIGD
     IIGVIDGIAF QTNILALNAA VEAARAGEQG RGFAVVAAEV RSLAQRSATA AKEIKALIET
     STQTVEEGAS LVTNAGSTMG EIVQSVRRVN EILDEISHAS REQSAGIEQV NRAVVEMDQV
     TQQNAALVEE AAAAAHSLKD QVDVLRDAIE SFSLPA
//
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