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Database: UniProt
Entry: A0A1H2M2M1_9ACTN
LinkDB: A0A1H2M2M1_9ACTN
Original site: A0A1H2M2M1_9ACTN 
ID   A0A1H2M2M1_9ACTN        Unreviewed;       734 AA.
AC   A0A1H2M2M1;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   RecName: Full=peptidoglycan glycosyltransferase {ECO:0000256|ARBA:ARBA00012555};
DE            EC=2.4.1.129 {ECO:0000256|ARBA:ARBA00012555};
GN   ORFNames=SAMN04488544_1301 {ECO:0000313|EMBL:SDU87513.1};
OS   Microlunatus sagamiharensis.
OC   Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC   Propionibacteriaceae; Microlunatus.
OX   NCBI_TaxID=546874 {ECO:0000313|EMBL:SDU87513.1, ECO:0000313|Proteomes:UP000198825};
RN   [1] {ECO:0000313|Proteomes:UP000198825}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 21743 {ECO:0000313|Proteomes:UP000198825};
RA   Varghese N., Submissions S.;
RL   Submitted (OCT-2016) 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; LT629799; SDU87513.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H2M2M1; -.
DR   STRING; 546874.SAMN04488544_1301; -.
DR   OrthoDB; 9766909at2; -.
DR   Proteomes; UP000198825; Chromosome i.
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:SDU87513.1}; 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:UP000198825};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        21..46
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          78..266
FT                   /note="Glycosyl transferase family 51"
FT                   /evidence="ECO:0000259|Pfam:PF00912"
FT   DOMAIN          369..641
FT                   /note="Penicillin-binding protein transpeptidase"
FT                   /evidence="ECO:0000259|Pfam:PF00905"
FT   REGION          688..734
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   734 AA;  77300 MW;  B56221CA535CADFA CRC64;
     MTPPTLTPAR RPRHVLRAGG LFVLVSVVCG LLVTAAALPL VGGAAWGAKE AREGMASLPL
     EFDAPAQSQR TRVLDADGKV IAYFYDQNRD YVTLDDIAPV MRTALISIED HRFYEHGPLD
     AQGTLRAFVT NLFAGGVTQG GSTLTQQYVK QVQVNAAALK GDESGVEAAT DSSYQRKLRE
     LRYAVSVEDT MSKDQILERY LNIAYFGGGA YGIEAASEHY FGTSAAKLTL PQAAMLAGLV
     QNPNGYDPVA HPDAGIQRRN VVLDRMAELG TASQAAVTKA KKSKFDAKAG DDVASGCQST
     DYPFICDYVK RTVLTMPSLG KTEKAREQAL MRGGLTIRTA IDPSTQDAVQ KAVSGAVGAK
     DPVIAAMDMI EPGTGRIIAM AQSRPVMGAS AKKGQTYWNY SVSPEMGGAQ GFQAGSTFKA
     FTAAAALEQG VPLSQRYDAK ARMDFSGARF DSCEGNVPIV GEFPVSNSTG VNGSMDMYRA
     ADFSVNTYFV QLALDVGMCD VTKMAEKLGV ESNTPGQPIS SYDSLPSFTL GTAETNPLSV
     ANAYATFASG GIHCDPVIVT KVTDSSGKSL EVPDAGCKRV ISEDVASAMD SLLSSVVTRG
     TGARARTADG RPQAGKTGTI DSNAAVWYAG YTPQVAGAAM ISIDKERKTP TSLKGYTVPS
     TSLYLEGSGS GDAGRRIWKP AMEQYLQGKP AEAFPSPPAD LVRGPSPFGR GQGTGQDGRD
     GEYGAGQQPG PGGR
//
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