ID D9UG45_STRS3 Unreviewed; 898 AA.
AC D9UG45;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, sequence version 1.
DT 24-JAN-2024, entry version 59.
DE RecName: Full=peptidoglycan glycosyltransferase {ECO:0000256|ARBA:ARBA00012555};
DE EC=2.4.1.129 {ECO:0000256|ARBA:ARBA00012555};
GN ORFNames=SSLG_03261 {ECO:0000313|EMBL:EFL01203.1};
OS Streptomyces sp. (strain SPB78).
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=591157 {ECO:0000313|EMBL:EFL01203.1, ECO:0000313|Proteomes:UP000005781};
RN [1] {ECO:0000313|EMBL:EFL01203.1, ECO:0000313|Proteomes:UP000005781}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SPB78 {ECO:0000313|EMBL:EFL01203.1,
RC ECO:0000313|Proteomes:UP000005781};
RG The Broad Institute Genome Sequencing Platform;
RG Broad Institute Microbial Sequencing Center;
RA Fischbach M., Godfrey P., Ward D., Young S., Zeng Q., Koehrsen M.,
RA Alvarado L., Berlin A.M., Bochicchio J., Borenstein D., Chapman S.B.,
RA Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A.,
RA Gujja S., Heilman E.R., Heiman D.I., Hepburn T.A., Howarth C., Jen D.,
RA Larson L., Lewis B., Mehta T., Park D., Pearson M., Richards J.,
RA Roberts A., Saif S., Shea T.D., Shenoy N., Sisk P., Stolte C., Sykes S.N.,
RA Thomson T., Walk T., White J., Yandava C., Straight P., Clardy J., Hung D.,
RA Kolter R., Mekalanos J., Walker S., Walsh C.T., Wieland-Brown L.C.,
RA Haas B., Nusbaum C., Birren B.;
RT "Annotation of Streptomyces sp. strain SPB78.";
RL Submitted (FEB-2009) 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};
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DR EMBL; GG657742; EFL01203.1; -; Genomic_DNA.
DR AlphaFoldDB; D9UG45; -.
DR STRING; 591157.SSLG_03261; -.
DR eggNOG; COG0744; Bacteria.
DR HOGENOM; CLU_006354_6_0_11; -.
DR Proteomes; UP000005781; 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:SF34; PENICILLIN-BINDING PROTEIN 1A; 1.
DR Pfam; PF00912; Transgly; 1.
DR Pfam; PF00905; Transpeptidase; 2.
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 114..137
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 164..334
FT /note="Glycosyl transferase family 51"
FT /evidence="ECO:0000259|Pfam:PF00912"
FT DOMAIN 456..519
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
FT DOMAIN 549..732
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
FT REGION 1..96
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 355..376
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 793..898
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 29..46
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 807..841
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 898 AA; 95921 MW; 69B0A70638C8144A CRC64;
MSEHRRKPPQ PEGGGRAAAR RARSGNTGRR ATPRGSAPSS SAHGSAGVEP PSHGGGRAEA
RRAAQRGSGG RRRAAPAAGQ GGGRRGGPPA KKRFIDYPRA GKDGVGRWLP SWKLVTGLFV
AFIGGLMGIA GIAYAMVEVP DEALSARAQN NVYYWSDGSQ MVATGGESQR NRQIVPLDQI
DKSMQYAVIS AENKSFETDS GVDPMGIGRA LFNMAKGGQT QGGSTITQQY VKNAVLDDQE
QTLSRKFKEL FISIKVGTTK SKDEIMAGYL NTAYYGRGAY GIQAASRAYF DKDAVDLNAS
ESALLAAVLK GATYYDPAGV ASDNPAKTTK EANTLRATER WSWILDEEVK DGHLGKSERD
KYTDLPKTEP PRANSALGGQ VGYLVELANS WVTSHSEDTG ITQNKLNQGG YRIYTTFKKD
RVKELEKSVS KVYNANIDPK KRPKTDKHVQ FGGASVNANT GAIEAIYGGT DALKHWTNNA
DVTGAQVGST FKPFVLAAAM EHGVRDPKLG ANQGDSTRRP VSQMSIFSAK NKLKIKNYDG
TIWTDKNGDQ WLQSNDGNES YHSDDNYRIT LREAMQHSVN SAFVQLGMDV GLDKVKDAAI
KAGIQDGPNI FASNNYPSFS LGTSSPSAIR MAGAYATFAN EGEQNDPYSV TKVESEKGTL
FQHKKKSKFA FPKPVADNVT DVLKNVVDKG TGTSAKIPGR DVAGKTGTTD GNKSAWFVGY
TPQVSTAIAM FRFDDNAKNK QREFEKMYGT GNQTSIHGAS FPAEIWKDYM TLALKDAPTE
NFPKPEKIGE VVETVDAPPS PSTKPSESPS ESPSKSPSQS PSSEAPPSPS TTESENTCAP
LDFNCQHGGD DEGPGGGDDQ GGDNQGPGQT SGPPSPSLPG EGDPGGDGDN GDNGWFKP
//
