ID M9R6H7_9RHOB Unreviewed; 649 AA.
AC M9R6H7;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE SubName: Full=Glycosyl transferase-like protein {ECO:0000313|EMBL:AGI67368.1};
GN ORFNames=OAN307_c17010 {ECO:0000313|EMBL:AGI67368.1};
OS Octadecabacter antarcticus 307.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Octadecabacter.
OX NCBI_TaxID=391626 {ECO:0000313|EMBL:AGI67368.1, ECO:0000313|Proteomes:UP000005307};
RN [1] {ECO:0000313|EMBL:AGI67368.1, ECO:0000313|Proteomes:UP000005307}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=307 {ECO:0000313|EMBL:AGI67368.1,
RC ECO:0000313|Proteomes:UP000005307};
RX PubMed=23671678;
RA Vollmers J., Voget S., Dietrich S., Gollnow K., Smits M., Meyer K.,
RA Brinkhoff T., Simon M., Daniel R.;
RT "Poles Apart: Arctic and Antarctic Octadecabacter strains Share High Genome
RT Plasticity and a New Type of Xanthorhodopsin.";
RL PLoS ONE 8:E63422-E63422(2013).
CC -!- SIMILARITY: Belongs to the glycosyltransferase 2 family.
CC {ECO:0000256|ARBA:ARBA00006739}.
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DR EMBL; CP003740; AGI67368.1; -; Genomic_DNA.
DR RefSeq; WP_015499400.1; NC_020911.1.
DR AlphaFoldDB; M9R6H7; -.
DR STRING; 391626.OAN307_c17010; -.
DR KEGG; oat:OAN307_c17010; -.
DR eggNOG; COG1215; Bacteria.
DR HOGENOM; CLU_020629_0_0_5; -.
DR OrthoDB; 7431422at2; -.
DR Proteomes; UP000005307; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR InterPro; IPR001173; Glyco_trans_2-like.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR InterPro; IPR037257; T2SS_E_N_sf.
DR InterPro; IPR007831; T2SS_GspE_N.
DR PANTHER; PTHR43630; POLY-BETA-1,6-N-ACETYL-D-GLUCOSAMINE SYNTHASE; 1.
DR PANTHER; PTHR43630:SF1; POLY-BETA-1,6-N-ACETYL-D-GLUCOSAMINE SYNTHASE; 1.
DR Pfam; PF13632; Glyco_trans_2_3; 1.
DR Pfam; PF05157; MshEN; 1.
DR SUPFAM; SSF160246; EspE N-terminal domain-like; 1.
DR SUPFAM; SSF53448; Nucleotide-diphospho-sugar transferases; 1.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Transferase {ECO:0000313|EMBL:AGI67368.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 191..211
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 217..238
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 507..531
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 551..572
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 60..164
FT /note="Type II secretion system protein GspE N-terminal"
FT /evidence="ECO:0000259|Pfam:PF05157"
FT DOMAIN 343..535
FT /note="Glycosyltransferase 2-like"
FT /evidence="ECO:0000259|Pfam:PF13632"
FT REGION 623..649
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 632..649
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 649 AA; 71962 MW; 912E37656173D044 CRC64;
MALTFSTVRQ RKLPAKNDLA NKLAAPRATG DVLGDNGVGA ARAFTQKDVN RRGSVAIAVA
LGHRLGLPST NPEQIEAGLA ETCVVDPVIT PADPRLIERF GAELCLKHRV LPWRSVSGRV
TVLATSPDHF LRIRDALVVV FGPIHLAIVT TNNLDAALSR MCHKALMRNA ELRTQQHESC
RDWNTGKAFR WGLGVVLAIM SCLIVWPQIS FFVLCGWAVF TLILKTILKV AAAVVHLFPK
PTSPMPANPQ LAHLPIVTIL VPLFRERDIA GTLIERLSRL DYPTDRLDVC LVLEADDGTT
QNALAATQLP FWMRAIKVPL GTLQTKPRAL NYALCFAKGS IIGVYDAEDA PAPDQIHIVV
NRFAQRGQDV ACLQGQLDFY NSHSNWLARC FTVEYATWFR IMLPGLERLG LAIPLGGTTL
FFRREILEEL GGWDAHNVTE DADLGIRLAR HGYRTEIIDT VTQEEANARA WPWIKQRSRW
LKGYAITYGV HMRSPLKLWR DLGAWRFFGL QLLFAGTISQ FLLAPLLWSF WLMLLGLPHP
LDNVLSTNVT LTFAAIFLLS EIINITVSAI AVTSPGKYDL IKWTPTLHFY FPLAALAAYK
GVIELATKPF YWDKTSHGIF APTQPAPTSP AARATNAPPE PPQRPIAAE
//
