ID E8JRC4_STREI Unreviewed; 773 AA.
AC E8JRC4;
DT 05-APR-2011, integrated into UniProtKB/TrEMBL.
DT 05-APR-2011, sequence version 1.
DT 27-MAR-2024, entry version 58.
DE RecName: Full=peptidoglycan glycosyltransferase {ECO:0000256|ARBA:ARBA00012555};
DE EC=2.4.1.129 {ECO:0000256|ARBA:ARBA00012555};
GN ORFNames=HMPREF0819_1547 {ECO:0000313|EMBL:EFW88376.1};
OS Streptococcus equinus ATCC 9812.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=525379 {ECO:0000313|EMBL:EFW88376.1, ECO:0000313|Proteomes:UP000005699};
RN [1] {ECO:0000313|EMBL:EFW88376.1, ECO:0000313|Proteomes:UP000005699}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 9812 {ECO:0000313|EMBL:EFW88376.1,
RC ECO:0000313|Proteomes:UP000005699};
RA Muzny D., Qin X., Deng J., Jiang H., Liu Y., Qu J., Song X.-Z., Zhang L.,
RA Thornton R., Coyle M., Francisco L., Jackson L., Javaid M., Korchina V.,
RA Kovar C., Mata R., Mathew T., Ngo R., Nguyen L., Nguyen N., Okwuonu G.,
RA Ongeri F., Pham C., Simmons D., Wilczek-Boney K., Hale W., Jakkamsetti A.,
RA Pham P., Ruth R., San Lucas F., Warren J., Zhang J., Zhao Z., Zhou C.,
RA Zhu D., Lee S., Bess C., Blankenburg K., Forbes L., Fu Q., Gubbala S.,
RA Hirani K., Jayaseelan J.C., Lara F., Munidasa M., Palculict T., Patil S.,
RA Pu L.-L., Saada N., Tang L., Weissenberger G., Zhu Y., Hemphill L.,
RA Shang Y., Youmans B., Ayvaz T., Ross M., Santibanez J., Aqrawi P.,
RA Gross S., Joshi V., Fowler G., Nazareth L., Reid J., Worley K.,
RA Petrosino J., Highlander S., Gibbs R.;
RL Submitted (DEC-2010) to the EMBL/GenBank/DDBJ databases.
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:EFW88376.1}.
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DR EMBL; AEVB01000037; EFW88376.1; -; Genomic_DNA.
DR RefSeq; WP_003067915.1; NZ_GL698434.1.
DR AlphaFoldDB; E8JRC4; -.
DR eggNOG; COG0744; Bacteria.
DR HOGENOM; CLU_006354_2_0_9; -.
DR Proteomes; UP000005699; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
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; 3.40.50.12800; -; 1.
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; NF038274; strep_PBP1B; 1.
DR PANTHER; PTHR32282; BINDING PROTEIN TRANSPEPTIDASE, PUTATIVE-RELATED; 1.
DR PANTHER; PTHR32282:SF32; PENICILLIN-BINDING PROTEIN 2A; 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 Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 35..56
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 88..275
FT /note="Glycosyl transferase family 51"
FT /evidence="ECO:0000259|Pfam:PF00912"
FT DOMAIN 401..635
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
SQ SEQUENCE 773 AA; 84208 MW; 325FE21A2E9C0CA6 CRC64;
MSKRTKHKKK ADYQKLGLLD FGSVFLRTVK LLTDFFYIIV ILFGMLGVGL AFGYLASQID
AVKVPDKDSL VSQVTSLTRV SQMSYSDGSS IAAIDTDLLR TPVASDAISE NIKHAIVATE
DENFEGHDGV VPKAVFRATL GSVLGLGETS GGSTLTQQLI KQQILGDDPT FKRKSREIIY
ALALERYLSK DEILTDYLNV SPFGRNNKGE NIAGIEEAAQ GIFGVSANDL TIPQAAFLAG
LPQSPIVYSP YTATGKLKDA DNMSYGLSRQ QDVLYNMYRA GYLTKDEYNE YKSYDISQDF
IQPASASTSY HDFLYYSVLE EAQDIMYDYL IEKNGVSEQE LKNDATKESY RKLASDTLQQ
GGYKVKTTID KNVYNAMQNA VSQYGSTLDQ GSSQTVDVGN VLMDNSTGAI LGFIGGRDYS
TNQNNHAFDT ARSPGSSIKP IIAYGIAIDQ GLLGSASMLS NYPTNFSSGQ PIMHGNDVGT
GMINLQEALN VSWNIPAYWT YQMLLNNNVD VESYMKKMGY SIVNYNIESL PLGGGIETTV
LQQVNAYQMI SNGGVYLKGY LVDSITDNQG NVIYKHKANP VRVFSEATAS ILNQLLKEVV
TGGATTEFYK DLQAINGSAA QADWSGKTGT TDNYTDVWLM LSTPKVTLGG WAGNDDNTSL
DSMAGYRYNA QYMANLVNSI YNANSNTFGT GKYNLSSNVM KSTVLKATGL QPGTVTVNGR
SLNVSGETTT SYWAKTGAGN MTYKFAIGGT DSDYTKAWDA LLHNSSIKTN NSN
//
