ID K2AHH0_9BACT Unreviewed; 1000 AA.
AC K2AHH0;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 48.
DE RecName: Full=peptidoglycan glycosyltransferase {ECO:0000256|ARBA:ARBA00012555};
DE EC=2.4.1.129 {ECO:0000256|ARBA:ARBA00012555};
GN ORFNames=ACD_63C00158G0002 {ECO:0000313|EMBL:EKD49394.1};
OS uncultured bacterium.
OC Bacteria; environmental samples.
OX NCBI_TaxID=77133 {ECO:0000313|EMBL:EKD49394.1};
RN [1] {ECO:0000313|EMBL:EKD49394.1}
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 -!- 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:EKD49394.1}.
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DR EMBL; AMFJ01026656; EKD49394.1; -; Genomic_DNA.
DR AlphaFoldDB; K2AHH0; -.
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 Gene3D; 2.60.40.10; Immunoglobulins; 2.
DR InterPro; IPR012338; Beta-lactam/transpept-like.
DR InterPro; IPR017868; Filamin/ABP280_repeat-like.
DR InterPro; IPR001264; Glyco_trans_51.
DR InterPro; IPR013783; Ig-like_fold.
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:SF33; PEPTIDOGLYCAN GLYCOSYLTRANSFERASE; 1.
DR Pfam; PF17957; Big_7; 2.
DR Pfam; PF00912; Transgly; 1.
DR Pfam; PF00905; Transpeptidase; 1.
DR SUPFAM; SSF56601; beta-lactamase/transpeptidase-like; 1.
DR SUPFAM; SSF53955; Lysozyme-like; 1.
DR PROSITE; PS50194; FILAMIN_REPEAT; 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 73..96
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 126..298
FT /note="Glycosyl transferase family 51"
FT /evidence="ECO:0000259|Pfam:PF00912"
FT DOMAIN 388..676
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
FT REGION 775..795
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1000 AA; 109789 MW; 9033ACBEAF849BAE CRC64;
MLKYGREVAH PYLKNCLLAT SLVKYTHSMS KNHNKIINLK TSKKSAGDLY RSKNKKRKSA
RRLSKKQKRA RRIFKTLVII LIVLLVAIGG VFAWGATQLP SSEEILSGRF VPQATQILDR
TGEHILFELH GEENRTLIKL MDLPEYIPQA SIAIEDDDFY KHPGFDVKGI IRAAWKNVTG
QQVSQGGSTI TQQLIKNTML TSDRTFTRKF KELVLSMELE MKLSKKEILE LYINAIPYGS
NAYGIQAASQ TYFGKDAKAL TIGEATMLAA LPKAPTYYSP LNHPERAKER QSLVIDRMRS
LGYITKEQAI EAKSEKLAFV KKRADITAPH FVDYAKEVLV EKYGLKKVET GGLKVYTTLD
LEKQKIAEGA VARHRKENEK IGAYNAAFLS LDSKTGEILA MVGSVDYFAE EGKKLDGQVN
VTTSLRSPGS SIKPVEYVTA FSRGYPPTTI LYDVKTNFGP DGSGKDYIPS NYSGSFSGPL
SMRTALAHSL NIPAIKTYYL AGPENVSTMA NKLGYHDWIP GKQYGLATAV GGKEIVMLDH
AGAYVTYANR GVRHTPTGIL KVIDSDGKVM EELDVSKGER VLDENIADTI NDVLADNNAR
APWGRQSLNI KDRQVAAKTG TSNKQINETI KPDNLWTIGY TPQIAAAVWV GNNDGSVTSG
QSDGSLNAAP IWREYMTKVL EKYPKEDFVK PKPINATKPV LLGKINGGEE TEIEICKPSG
LLANKYCPNS MKEKKKFRRN AHCILYYVDK NDPNGPPPKN PAEDPQFKRW EAAVRGGSDN
NTETDNPPTE EDTLHNPEFW PNISIISPED GANITSGIFS ASVNVSGTNP IKHVEYFIDG
KRVADTNSAP YGVEIVVPAG ITQGFHQLTA KVYDNIDNSK TASININFKA TNVKPSISMT
SPSSGTNIPV GESVIVSAHA TGNSDLRVEF FVQYPDGSTA TLGGDSSPDG DGNYGTSWTP
SRAGKHYLWA TVTDKNNNNA QSSKVSVTVT GVNAMLQMLI
//
