ID F0M3E9_PSEPM Unreviewed; 770 AA.
AC F0M3E9;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 03-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 71.
DE RecName: Full=peptidoglycan glycosyltransferase {ECO:0000256|ARBA:ARBA00012555};
DE EC=2.4.1.129 {ECO:0000256|ARBA:ARBA00012555};
DE Flags: Precursor;
GN OrderedLocusNames=Asphe3_33170 {ECO:0000313|EMBL:ADX74424.1};
OS Pseudarthrobacter phenanthrenivorans (strain DSM 18606 / JCM 16027 / LMG
OS 23796 / Sphe3) (Arthrobacter phenanthrenivorans).
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC Pseudarthrobacter.
OX NCBI_TaxID=930171 {ECO:0000313|EMBL:ADX74424.1, ECO:0000313|Proteomes:UP000008639};
RN [1] {ECO:0000313|EMBL:ADX74424.1, ECO:0000313|Proteomes:UP000008639}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 18606 / JCM 16027 / LMG 23796 / Sphe3
RC {ECO:0000313|Proteomes:UP000008639};
RX PubMed=21677849; DOI=10.4056/sigs.1393494;
RA Kallimanis A., Labutti K.M., Lapidus A., Clum A., Lykidis A.,
RA Mavromatis K., Pagani I., Liolios K., Ivanova N., Goodwin L., Pitluck S.,
RA Chen A., Palaniappan K., Markowitz V., Bristow J., Velentzas A.D.,
RA Perisynakis A., Ouzounis C.C., Kyrpides N.C., Koukkou A.I., Drainas C.;
RT "Complete genome sequence of Arthrobacter phenanthrenivorans type strain
RT (Sphe3).";
RL Stand. Genomic Sci. 4:123-130(2011).
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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP002379; ADX74424.1; -; Genomic_DNA.
DR AlphaFoldDB; F0M3E9; -.
DR STRING; 930171.Asphe3_33170; -.
DR KEGG; apn:Asphe3_33170; -.
DR eggNOG; COG0744; Bacteria.
DR HOGENOM; CLU_006354_2_6_11; -.
DR Proteomes; UP000008639; Chromosome.
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:SF33; PEPTIDOGLYCAN GLYCOSYLTRANSFERASE; 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:ADX74424.1}; 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 Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 21..44
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 80..267
FT /note="Glycosyl transferase family 51"
FT /evidence="ECO:0000259|Pfam:PF00912"
FT DOMAIN 368..648
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
FT REGION 717..770
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 719..738
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 755..770
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 770 AA; 81300 MW; DA0CBBE84B59C215 CRC64;
MENMATRTNP LFDTATTLGK ILVFLGVSAI CGVLVAGLLV PAAAVSGSAA SGSIEFFDTL
PAELKVDPPN QTTRILAADG SEIASVYTEN RTKVALDQIS PFMKEAVIAV EDSRFYDHGG
VDTTGILRAL VSTARGNRQG ASTITQQYVN NVLNANLAAE GNEDQIKLNG VNKGVGDKLR
EMKLAIALEK EFSKEQILEG YLNIVFFNRD AYGVEAASRF FFSTSAKDLT LPQAALLAGL
VNSPSAFDPI NNPESSKQRR DLVLTLMRDQ GKITQADYEA AVATPVETKV TPARQGCAYA
STAPYFCDYV LHLLENNPAY GEDLKERQRL IYGGGLTITT TLDPNAQAVA QEQVNASAGA
NPDKWGAAMV SVQPNSGKII SMAQNTSFLP AEGAFDSQVN FNVDKLDKDG NDLNGLGGAQ
PGSTMKPFTF AQWLNEGKSM NTVVNAAQRR YPLNFPWRNS CGQVTGAYNT AQKALGAADD
LQNAEPQWYR PLSVLEGLYN SINTVTFASA AQLDFCGIQK IVDATGLHGG LPADGDPNPK
INMSTLGNLL GSTQTAPLTM ASAFATFAND GKYCEPIAIT SVTDQTGATL PAQSTSCRDA
VKPEVARGVN YALQEVLNRG SGSLIQPRIS TRTSFPIGAK TGTSNNNGST WVVGHTTGLA
TAAWFGDALG AQDRSGQNIT VNGKFYPGID GYMIAGPMFS NFMSRVAPAY GTEPFPAPPS
NLLNGTTRST TPATTAPQAT RAPAPAPAAP QPAPQPTNNG NGNGNGNNDD
//
