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Database: UniProt
Entry: K2AI20_9BACT
LinkDB: K2AI20_9BACT
Original site: K2AI20_9BACT 
ID   K2AI20_9BACT            Unreviewed;       596 AA.
AC   K2AI20;
DT   28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT   28-NOV-2012, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EKD61302.1};
GN   ORFNames=ACD_54C00299G0005 {ECO:0000313|EMBL:EKD61302.1};
OS   uncultured bacterium.
OC   Bacteria; environmental samples.
OX   NCBI_TaxID=77133 {ECO:0000313|EMBL:EKD61302.1};
RN   [1] {ECO:0000313|EMBL:EKD61302.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=23019650; DOI=10.1126/science.1224041;
RA   Wrighton K.C., Thomas B.C., Sharon I., Miller C.S., Castelle C.J.,
RA   VerBerkmoes N.C., Wilkins M.J., Hettich R.L., Lipton M.S., Williams K.H.,
RA   Long P.E., Banfield J.F.;
RT   "Fermentation, hydrogen, and sulfur metabolism in multiple uncultivated
RT   bacterial phyla.";
RL   Science 337:1661-1665(2012).
CC   -!- SIMILARITY: Belongs to the glycosyltransferase 2 family.
CC       {ECO:0000256|ARBA:ARBA00006739}.
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:EKD61302.1}.
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DR   EMBL; AMFJ01023068; EKD61302.1; -; Genomic_DNA.
DR   AlphaFoldDB; K2AI20; -.
DR   GO; GO:0016020; C:membrane; 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   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        167..184
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        190..211
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        481..502
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        522..544
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        556..576
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          38..137
FT                   /note="Type II secretion system protein GspE N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05157"
FT   DOMAIN          317..507
FT                   /note="Glycosyltransferase 2-like"
FT                   /evidence="ECO:0000259|Pfam:PF13632"
SQ   SEQUENCE   596 AA;  66961 MW;  056FDC6C8668A1CC CRC64;
     MKTFAAVLLQ DGLVAPHAMT QVLALRDQLG RHLTDILLAR EVLPALTLYE AIAQHWQVSV
     ADLAKRPPDP RLMQQLGTVD ALTNGLLPWC KAGQVTVVAT AYPDQFQRHK PRLEAAFGPV
     AMAVAPMHQI ETAVLALHGP RLARAAETRV APEESCRNYH STTLQRPALL LASILAIFAF
     FQPLGFLFTA FGLAILAMLA ANVMKVIALL LMHRPEPAAQ NPPFVAHLPT VSIIVALYRE
     SDIAPRLAAR LGKLDYPRDL LDILLVVEAE DQLTRTALHH ADLPGWMRVI VVPDGSVKTK
     PRALNYALDH CRGSIIGVYD AEDAPESDQI RKVVDRFHQR GPEVVCLQGV LDFYNPRSNW
     LARCFTIEYA SWFRMYLPGI ERMGLAVPLG GTTLFFRRRA LEALGGWDAQ NVTEDADLGL
     RLARHGYRTE LIDTTTFEEP NCRSLPWVKQ RSRWIKGYMM TWLTHMRNPR LLWTQLGPRR
     FIGLQVQFLG SVLQSLLAPL LWSFWLVPFG VPHPVVQTIN PAAFTLLYVS MFAVSALTIG
     FDIAGMRRTK HRLNPLWAVS LTFYHPLGTL AAYKALWELL TKPFYWDKTS HGHFDL
//
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