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Database: UniProt
Entry: A0A0R1HS45_9LACO
LinkDB: A0A0R1HS45_9LACO
Original site: A0A0R1HS45_9LACO 
ID   A0A0R1HS45_9LACO        Unreviewed;       748 AA.
AC   A0A0R1HS45;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 35.
DE   RecName: Full=peptidoglycan glycosyltransferase {ECO:0000256|ARBA:ARBA00012555};
DE            EC=2.4.1.129 {ECO:0000256|ARBA:ARBA00012555};
GN   ORFNames=FC66_GL000695 {ECO:0000313|EMBL:KRK46194.1};
OS   Dellaglioa algida DSM 15638.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Dellaglioa.
OX   NCBI_TaxID=1423719 {ECO:0000313|EMBL:KRK46194.1, ECO:0000313|Proteomes:UP000051450};
RN   [1] {ECO:0000313|EMBL:KRK46194.1, ECO:0000313|Proteomes:UP000051450}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 15638 {ECO:0000313|EMBL:KRK46194.1,
RC   ECO:0000313|Proteomes:UP000051450};
RX   PubMed=26415554; DOI=10.1038/ncomms9322;
RA   Sun Z., Harris H.M., McCann A., Guo C., Argimon S., Zhang W., Yang X.,
RA   Jeffery I.B., Cooney J.C., Kagawa T.F., Liu W., Song Y., Salvetti E.,
RA   Wrobel A., Rasinkangas P., Parkhill J., Rea M.C., O'Sullivan O., Ritari J.,
RA   Douillard F.P., Paul Ross R., Yang R., Briner A.E., Felis G.E.,
RA   de Vos W.M., Barrangou R., Klaenhammer T.R., Caufield P.W., Cui Y.,
RA   Zhang H., O'Toole P.W.;
RT   "Expanding the biotechnology potential of lactobacilli through comparative
RT   genomics of 213 strains and associated genera.";
RL   Nat. Commun. 6:8322-8322(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:KRK46194.1}.
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DR   EMBL; AZDI01000002; KRK46194.1; -; Genomic_DNA.
DR   RefSeq; WP_057973770.1; NZ_AZDI01000002.1.
DR   AlphaFoldDB; A0A0R1HS45; -.
DR   STRING; 1423719.FC66_GL000695; -.
DR   PATRIC; fig|1423719.4.peg.705; -.
DR   Proteomes; UP000051450; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; 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:0009002; F:serine-type D-Ala-D-Ala carboxypeptidase 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:SF29; PENICILLIN-BINDING PROTEIN 1A; 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:KRK46194.1}; 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   Reference proteome {ECO:0000313|Proteomes:UP000051450};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        20..45
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          77..247
FT                   /note="Glycosyl transferase family 51"
FT                   /evidence="ECO:0000259|Pfam:PF00912"
FT   DOMAIN          344..590
FT                   /note="Penicillin-binding protein transpeptidase"
FT                   /evidence="ECO:0000259|Pfam:PF00905"
SQ   SEQUENCE   748 AA;  82661 MW;  95561BB994F38866 CRC64;
     MEKQEKIKKT KWRYRHPHIF RYVAIFSVLL LLGVAAISLY VAAVIKSVPT VTSQELISDA
     SSNMYDREGQ LIWSSALNKR VYVKAKDIPK IYSDLLLSTE DQTFYKDAGF SPSGLANAAF
     STVKSAVGKG EVRGGSSIEQ QLIKLTVFST SNKDRTVDRK IKEFFLAQQL YHNYSKDQIL
     EFYINKMSLG EGSYGAQTIS ETYFGKTLKQ LSVSQQAIIA GLGQAPSTYN LYSNPKAVRA
     RRNIVLKTGL ENKVITKSQY KIAIAESVTK DLKKRHWMEN SVTKKILENN AYVTSALEQV
     SDKGYDLSKT PLQINTALDS SKNAYVKKLA DDEKYYQDST EQSAITITDP KTGNIVAQYG
     GRHQKTAFSY NRAISTQRSS GSGIKPLLDY GPAIEYFGWA TTHALDGTAY AYRGTNLLAQ
     NFDDVSYRSI TMQNALRVSA NTPAIRTLDT VGSAKAAQFL TQIGMPQTNA PAGSQAIGLD
     VSTEQMATAY GAVSNGGTYH AARYVTSLKF SDNSVKKYDV IGKRAMKAST AFILTSMMEG
     VPNAGGTAPN AKINGIHQAM KTGTVGYSAA AKFPENANMD VWMNGFTKST SVSMWLGYDE
     PMKKGHYITD AASAMTNVNL YRDLMEHFSK ENDADNSEWE KPSTVNQLSG IGLSAQYEPN
     DKVVVLGVKE PETIDLKKAK VYKTYLSKTI DKDILKVKFE DIAYQKKPDS YKIGSWKKDT
     NDKLDLTQKK LDKANDGIKS AKEMLEGE
//
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