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Database: UniProt
Entry: A0A0G0NGA2_9BACT
LinkDB: A0A0G0NGA2_9BACT
Original site: A0A0G0NGA2_9BACT 
ID   A0A0G0NGA2_9BACT        Unreviewed;       821 AA.
AC   A0A0G0NGA2;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   27-MAR-2024, entry version 33.
DE   RecName: Full=peptidoglycan glycosyltransferase {ECO:0000256|ARBA:ARBA00012555};
DE            EC=2.4.1.129 {ECO:0000256|ARBA:ARBA00012555};
GN   ORFNames=UT39_C0002G0027 {ECO:0000313|EMBL:KKR11846.1};
OS   Candidatus Woesebacteria bacterium GW2011_GWA1_39_21.
OC   Bacteria; Candidatus Woesebacteria.
OX   NCBI_TaxID=1618550 {ECO:0000313|EMBL:KKR11846.1, ECO:0000313|Proteomes:UP000034246};
RN   [1] {ECO:0000313|EMBL:KKR11846.1, ECO:0000313|Proteomes:UP000034246}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Brown C.T., Hug L.A., Thomas B.C., Sharon I., Castelle C.J., Singh A.,
RA   Wilkins M.J., Williams K.H., Banfield J.F.;
RT   "rRNA introns, odd ribosomes, and small enigmatic genomes across a large
RT   radiation of phyla.";
RL   Nature 0:0-0(2015).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-
CC         Ala)](n)-di-trans,octa-cis-undecaprenyl diphosphate + beta-D-GlcNAc-
CC         (1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-di-trans,octa-
CC         cis-undecaprenyl diphosphate = [GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-
CC         D-Glu-L-Lys-D-Ala-D-Ala)](n+1)-di-trans-octa-cis-undecaprenyl
CC         diphosphate + di-trans,octa-cis-undecaprenyl diphosphate + H(+);
CC         Xref=Rhea:RHEA:23708, Rhea:RHEA-COMP:9602, Rhea:RHEA-COMP:9603,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:58405, ChEBI:CHEBI:60033,
CC         ChEBI:CHEBI:78435; EC=2.4.1.129;
CC         Evidence={ECO:0000256|ARBA:ARBA00023988};
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:KKR11846.1}.
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DR   EMBL; LBWP01000002; KKR11846.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0G0NGA2; -.
DR   STRING; 1618550.UT39_C0002G0027; -.
DR   PATRIC; fig|1618550.3.peg.125; -.
DR   Proteomes; UP000034246; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0004180; F:carboxypeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008658; F:penicillin binding; IEA:InterPro.
DR   GO; GO:0008955; F:peptidoglycan glycosyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.3810.10; Biosynthetic peptidoglycan transglycosylase-like; 1.
DR   Gene3D; 3.40.710.10; DD-peptidase/beta-lactamase superfamily; 1.
DR   InterPro; IPR012338; Beta-lactam/transpept-like.
DR   InterPro; IPR001264; Glyco_trans_51.
DR   InterPro; IPR023346; Lysozyme-like_dom_sf.
DR   InterPro; IPR036950; PBP_transglycosylase.
DR   InterPro; IPR001460; PCN-bd_Tpept.
DR   PANTHER; PTHR32282; BINDING PROTEIN TRANSPEPTIDASE, PUTATIVE-RELATED; 1.
DR   PANTHER; PTHR32282:SF33; PEPTIDOGLYCAN GLYCOSYLTRANSFERASE; 1.
DR   Pfam; PF00912; Transgly; 1.
DR   Pfam; PF00905; Transpeptidase; 1.
DR   SUPFAM; SSF56601; beta-lactamase/transpeptidase-like; 1.
DR   SUPFAM; SSF53955; Lysozyme-like; 1.
PE   4: Predicted;
KW   Carboxypeptidase {ECO:0000256|ARBA:ARBA00022645};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW   Protease {ECO:0000256|ARBA:ARBA00022670};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        99..118
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          142..317
FT                   /note="Glycosyl transferase family 51"
FT                   /evidence="ECO:0000259|Pfam:PF00912"
FT   DOMAIN          404..676
FT                   /note="Penicillin-binding protein transpeptidase"
FT                   /evidence="ECO:0000259|Pfam:PF00905"
SQ   SEQUENCE   821 AA;  90887 MW;  4B60082D737AC8B4 CRC64;
     MSIKMKNKKV LKKRKALVEH TKIVDENLTK TKTSTLKKLS SFFWTVFQKV GKYLFLSIYH
     LLKYIYQLPL KIFYKRKGPN PRKDQKAGKS PLANNRLRFT LFFLVLAAAV VFFTWLFWGL
     PLPTKLLQTQ VPVSTKIYDR TGKPIYEIYT DKRSTPVDVD SLPSYVVDAT ISIEDKDFYK
     HHGISLTGIA RAAYNTVFKQ KLQGGSTLTQ QLVKNALLTP DRTIKRKLRE IVITVFVEAM
     YSKKQILSMY FNQIPYGSTA YGIGAASELY FNKEAKDLTL SEAALLAGIT AAPTKYSPFG
     AHPEIAKTRQ ELVLRRMVED GLISSGQADE ANSEKLNYAE PEKFKAPHFS LWVKELLADK
     YGDAVVEQGG LRVITTLDLD LQEYAEATVS AELAKLKKQN VRNGAVLVTR PKSGEILAMV
     GSKDYFAKDE DGKFNVILAN RQPGSSIKPL NYALALRDKK ITLSTPLADV PTCFNVFGQK
     EYCPVNYDGT FHGAVQPRFS LGNSYNVPAV RVLALNGLEN FIYFATNMGI TTLTDPKNYG
     LSLTLGGGEV KPYDMAVSFG VFANAGVKVP LNPILKVTDW KGKIYEDNNP NDVDGQRILD
     PDATFLISHV LYDNNARVAA FGPSSYLVVN GHPEVSVKTG TTNDRRDNWT IGYTPQVVVV
     VWVGNNDNSA MSGAVSGVSG ASPIWNKIIK YTLDKAEKGF YNQDDGHAWP GQPDNVVGRN
     VCATTGNLPA DESNPGCPTR FEYFLKDNIG ANVESGQRDL QIDKTTGMLA FPDTPPENIE
     TQNHPFLLDP LGTLVCLDCP IASESAKINY PLVNTTSTSV P
//
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