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Database: UniProt
Entry: G2GXI0_9ENTR
LinkDB: G2GXI0_9ENTR
Original site: G2GXI0_9ENTR 
ID   G2GXI0_9ENTR            Unreviewed;      1180 AA.
AC   G2GXI0;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 1.
DT   27-MAR-2024, entry version 35.
DE   SubName: Full=Glycosyltransferase {ECO:0000313|EMBL:EGY29542.1};
GN   ORFNames=Rin_00004720 {ECO:0000313|EMBL:EGY29542.1};
OS   Candidatus Regiella insecticola 5.15.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; aphid secondary symbionts; Regiella.
OX   NCBI_TaxID=1005043 {ECO:0000313|EMBL:EGY29542.1, ECO:0000313|Proteomes:UP000004116};
RN   [1] {ECO:0000313|EMBL:EGY29542.1, ECO:0000313|Proteomes:UP000004116}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=R5.15 {ECO:0000313|Proteomes:UP000004116};
RX   PubMed=21948522; DOI=10.1101/gr.125351.111;
RA   Hansen A.K., Vorburger C., Moran N.A.;
RT   "Genomic basis of endosymbiont-conferred protection against an insect
RT   parasitoid.";
RL   Genome Res. 22:106-114(2012).
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
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:EGY29542.1}.
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DR   EMBL; AGCA01000103; EGY29542.1; -; Genomic_DNA.
DR   RefSeq; WP_006706174.1; NZ_AGCA01000103.1.
DR   AlphaFoldDB; G2GXI0; -.
DR   OrthoDB; 5489595at2; -.
DR   Proteomes; UP000004116; Unassembled WGS sequence.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0033644; C:host cell membrane; IEA:UniProtKB-KW.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0016757; F:glycosyltransferase activity; IEA:InterPro.
DR   GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR   Gene3D; 1.20.140.180; -; 2.
DR   Gene3D; 3.40.50.11550; -; 1.
DR   Gene3D; 3.90.550.20; -; 1.
DR   InterPro; IPR020972; Dermonecrotic/RTX_toxin_MLD.
DR   InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR   InterPro; IPR024770; TcdA/TcdB_cat.
DR   InterPro; IPR048461; ToxA-like_C2.
DR   Pfam; PF11647; MLD; 1.
DR   Pfam; PF20899; PMT_C2; 1.
DR   Pfam; PF12919; TcdA_TcdB; 1.
DR   SUPFAM; SSF159501; EreA/ChaN-like; 1.
DR   SUPFAM; SSF53448; Nucleotide-diphospho-sugar transferases; 1.
DR   SUPFAM; SSF158842; PMT central region-like; 2.
PE   4: Predicted;
KW   Host membrane {ECO:0000256|ARBA:ARBA00022870};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136};
KW   Reference proteome {ECO:0000313|Proteomes:UP000004116};
KW   Secreted {ECO:0000256|ARBA:ARBA00022525};
KW   Toxin {ECO:0000256|ARBA:ARBA00022656};
KW   Transferase {ECO:0000313|EMBL:EGY29542.1};
KW   Virulence {ECO:0000256|ARBA:ARBA00023026}.
FT   DOMAIN          104..471
FT                   /note="GT44"
FT                   /evidence="ECO:0000259|Pfam:PF12919"
FT   DOMAIN          819..1056
FT                   /note="Dermonecrotic toxin-like C2"
FT                   /evidence="ECO:0000259|Pfam:PF20899"
FT   DOMAIN          1090..1145
FT                   /note="Dermonecrotic/RTX toxin membrane localization"
FT                   /evidence="ECO:0000259|Pfam:PF11647"
FT   REGION          1157..1180
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1180 AA;  135335 MW;  9ED261ABD66A4E19 CRC64;
     MTERNSHESS GIENNNQRHD YNEIKKAQTH YQEQLNSIQN SLEEWELLKE INQKIHRYIE
     KYPLVGSDEV EHLRSEEIKQ LLAQNQQRNR ELAIMPELRR EIPKKIHFVW LGKLGTIQQE
     YIRAWNEINK GENYTITIWY DKDALLVHEL NKRIKAFAKK INQLNFTPDA YANAVIVIQN
     QAYQKITEAL ERGLTFDQAS INFIRDYLKG DEQELRNIKK QNQASFDDFI LNERKAGRHY
     TLKNVKSLFD IDPHNPNPVQ DREIQIQQKN YQLELALRQN MAAASDMLRL KVLEQQGGGY
     FDADLLPAFK ADLWENLEIP AALSKSDLND TDFNLAKTQL VLEHLSEFFP HRKMLFDSNK
     YQDYAKSFAA KGSAHKKLID DMRIFLRGKR NTLSDFFQPL QPIKLHPDGI LVAKNRDVFI
     NNNAIFSYPN SGSIKLLQQQ IGNNYRFLRD HDLVFVDNTD VINDRINNYT DKITLALWND
     PKASTRINGE IGNMLFRKDG VVPGSQATIF ISGPEMFERR IKRYSEQMFG QQRNPLSSSA
     EASFFISGLF SDFNNFTEED MVSSWIQETE ASSQTLLIKR SDQLKEWSAL DIQNKPHQGN
     ANQEKLYNDI RHHFDTLFLE NTDKKILKNI FSLQLKIQSY INNYPKFPSV AALKELQKKI
     HNIVFPDADF KLNQQRSIII ISKIDPEQAA RIYMSIHDHN KYGKAEPNIN ALIFSDPYLQ
     PFKGFTGEEN DIFQGKQGDF NAKFHIPLGN KFTVFKANLL AAQAQNVLNN VYLDEKKIAH
     IGYSYNELTA LKGNEHVGII IYTIILAIQE KRDSNFIGQT DLLMLKNFAN QRYLQDMQRE
     RLADINQIGK SDPNTEIAEW DKHYSGQTGE QLQQRLLDKN LNINSWLDVL LENRKGLLIS
     ENNYGLDFVT RHLIGLKSKG ITTIGLGVLN AKFAQPLIDD YLRTGNLSGE LAVMVETNGL
     GKLFESAFAK KMKIIALGVD SRRKGIEEDD YENIYRIDKT NQGVVEAFNQ PGGKFVAILS
     SEFLQSQPGI EGPLSGITHR LGLPALTANE SGFTWLADNI YQRKAYQPLS LNSIEQSASF
     PHFSVTADPG YQNILSTLDE LHARVSNSGK INTACQLHQE IQQYIQRNPD SELNSRLITL
     KKQIAALFPS VELPFSPGRG QKRKMPSAIF DSHGSREGNT
//
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