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Database: UniProt
Entry: A0A0L0GVL5_9ENTR
LinkDB: A0A0L0GVL5_9ENTR
Original site: A0A0L0GVL5_9ENTR 
ID   A0A0L0GVL5_9ENTR        Unreviewed;       551 AA.
AC   A0A0L0GVL5;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   27-MAR-2024, entry version 39.
DE   SubName: Full=Chemotaxis protein {ECO:0000313|EMBL:KNC93140.1};
GN   ORFNames=GM31_20525 {ECO:0000313|EMBL:KNC93140.1};
OS   Trabulsiella odontotermitis.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Trabulsiella.
OX   NCBI_TaxID=379893 {ECO:0000313|EMBL:KNC93140.1, ECO:0000313|Proteomes:UP000037393};
RN   [1] {ECO:0000313|EMBL:KNC93140.1, ECO:0000313|Proteomes:UP000037393}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=12 {ECO:0000313|EMBL:KNC93140.1,
RC   ECO:0000313|Proteomes:UP000037393};
RX   PubMed=26162887;
RA   Sapountzis P., Gruntjes T., Otani S., Estevez J., da Costa R.R.,
RA   Plunkett G.3rd., Perna N.T., Poulsen M.;
RT   "The Enterobacterium Trabulsiella odontotermitis Presents Novel Adaptations
RT   Related to Its Association with Fungus-Growing Termites.";
RL   Appl. Environ. Microbiol. 81:6577-6588(2015).
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}.
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:KNC93140.1}.
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DR   EMBL; JNGI01000062; KNC93140.1; -; Genomic_DNA.
DR   RefSeq; WP_049857167.1; NZ_JNGI01000062.1.
DR   AlphaFoldDB; A0A0L0GVL5; -.
DR   PATRIC; fig|379893.4.peg.4166; -.
DR   OrthoDB; 9765776at2; -.
DR   Proteomes; UP000037393; 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   CDD; cd19407; Tar_Tsr_sensor; 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; IPR004091; Chemotax_Me-accpt_rcpt_Me-site.
DR   InterPro; IPR003660; HAMP_dom.
DR   InterPro; IPR004089; MCPsignal_dom.
DR   InterPro; IPR000727; T_SNARE_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   SMART; SM00319; TarH; 1.
DR   SUPFAM; SSF47170; Aspartate receptor, ligand-binding domain; 1.
DR   SUPFAM; SSF58104; Methyl-accepting chemotaxis protein (MCP) signaling domain; 1.
DR   PROSITE; PS00538; CHEMOTAXIS_TRANSDUC_1; 1.
DR   PROSITE; PS50111; CHEMOTAXIS_TRANSDUC_2; 1.
DR   PROSITE; PS50885; HAMP; 1.
DR   PROSITE; PS50192; T_SNARE; 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   Reference proteome {ECO:0000313|Proteomes:UP000037393};
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        192..214
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          216..268
FT                   /note="HAMP"
FT                   /evidence="ECO:0000259|PROSITE:PS50885"
FT   DOMAIN          273..502
FT                   /note="Methyl-accepting transducer"
FT                   /evidence="ECO:0000259|PROSITE:PS50111"
FT   DOMAIN          432..494
FT                   /note="T-SNARE coiled-coil homology"
FT                   /evidence="ECO:0000259|PROSITE:PS50192"
FT   REGION          531..551
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   551 AA;  59259 MW;  276B0F4DA72504B2 CRC64;
     MFKRIKVITL LITVLFVLGA MQLFSAGIFV KALNNDKNNF SVAQLSNENV AAFTDAWVSL
     NQARVTLNRG MLRLQSSMGT QINGGQLSEL VKTANDLLAE AKGHYDRYHE LPNTPGLDKN
     LTESLETQYG IYSATLARMT VLLDQGKLED MFKENAEQKQ QAMQKSYREW RAMQTQLTNA
     GIEDNNNDYS RILWILVTIM VIVVVAIVAS WVAMQRVLLK PLHQVMEHIR AIAAGDLTHP
     IDADGSNEMA LLAGNVREMQ QALAKTVTIV REGADTIYTG AGEISAGSND LSSRTEQQAA
     SLEETAASME QLTATVKQNA DNARQASGLA LTASKTAQKG GDVVDGVVRT MDEIARSSGQ
     ISQITSVIDG IAFQTNILAL NAAVEAARAG EQGRGFAVVA GEVRTLAQRS AQAAKEIKGL
     IEDSVERVST GSTLVHEAGE TMAEIVNSVT RVNDIMAEIA SASDEQSRGI DQVGQAIAEM
     DRVTQQNASL VEESAAAAAA LEEQSARLNE TVAVFKIPRS NAPKAVAARP MPTVKKPAPT
     LATADGNWET F
//
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