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Database: UniProt
Entry: A0A0G0KK53_9BACT
LinkDB: A0A0G0KK53_9BACT
Original site: A0A0G0KK53_9BACT 
ID   A0A0G0KK53_9BACT        Unreviewed;       636 AA.
AC   A0A0G0KK53;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   27-MAR-2024, entry version 31.
DE   RecName: Full=peptidoglycan glycosyltransferase {ECO:0000256|ARBA:ARBA00012555};
DE            EC=2.4.1.129 {ECO:0000256|ARBA:ARBA00012555};
GN   ORFNames=US69_C0004G0043 {ECO:0000313|EMBL:KKQ49559.1};
OS   candidate division TM6 bacterium GW2011_GWF2_38_10.
OC   Bacteria; Candidatus Dependentiae.
OX   NCBI_TaxID=1619084 {ECO:0000313|EMBL:KKQ49559.1, ECO:0000313|Proteomes:UP000034625};
RN   [1] {ECO:0000313|EMBL:KKQ49559.1, ECO:0000313|Proteomes:UP000034625}
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   -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC       {ECO:0000256|ARBA:ARBA00004752}.
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:KKQ49559.1}.
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DR   EMBL; LBTY01000004; KKQ49559.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0G0KK53; -.
DR   STRING; 1619084.US69_C0004G0043; -.
DR   PATRIC; fig|1619084.3.peg.270; -.
DR   Proteomes; UP000034625; Unassembled WGS sequence.
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   NCBIfam; TIGR02074; PBP_1a_fam; 1.
DR   PANTHER; PTHR32282; BINDING PROTEIN TRANSPEPTIDASE, PUTATIVE-RELATED; 1.
DR   PANTHER; PTHR32282:SF11; PENICILLIN-BINDING PROTEIN 1B; 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   ECO:0000313|EMBL:KKQ49559.1}; Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW   Protease {ECO:0000256|ARBA:ARBA00022670}.
FT   DOMAIN          50..225
FT                   /note="Glycosyl transferase family 51"
FT                   /evidence="ECO:0000259|Pfam:PF00912"
FT   DOMAIN          318..566
FT                   /note="Penicillin-binding protein transpeptidase"
FT                   /evidence="ECO:0000259|Pfam:PF00905"
SQ   SEQUENCE   636 AA;  71736 MW;  F7769D5516F1FCF5 CRC64;
     MVKKIVFGCF FLCCLGLGAL CYLLEKEWVN FSQLGYYSQA KPSIVLDDEG RELARFELDR
     RDPVTYDKIP DIIVKAFIAA EDHRFFEHPG ISFKGIIRSF LVNFYHGRVV QGASTITQQL
     ARGMFLYHDR TIWRKIQEVF IAFQLERQLS KEQILELYLN NIYFGQGTYG IEAACRRFWN
     ISLSDVTTAQ AATLAAVPAS AFLYSPLNAP CSAKKRRNVI IATMQRLGFI GEREALKAKD
     EKLVVLDSAQ GNPIRLYIIE WIRVWAESLW GREALYRQGL RIQTTINSDM QTAAEKSFNA
     VVAKMNKEME GNFNGGLISL DTATGKIRAA VGGLNFKASQ FNRTFQAYRQ MGSAFKPLLF
     AYALERGVEL DQVMIDEPFE LELANGQSWA PRNWHRRFEG PMTLVRALTV SNNVISVKLF
     LDLGIPEVVS WMRRFNFKNE LPPYPSAALG TIEATLEETS AAFNSIVNGG VLIKPYLVEW
     VKDCWGKKLW MAEPKSTRVM SRTTASKMIN ALSHRMELNK KRTKDGWIDA QSIGKTGSTN
     GAATTWFVGA TPSFTTAVYV GRDDNKPMGS RVYASATAYP IWLEFNKAIL HPKKEFYIDP
     SLHSVTIDWV TGQSGNYTSV LGYGDVLQKV AILKDL
//
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