ID   A0A0H5CRM4_9PSEU        Unreviewed;       747 AA.
AC   A0A0H5CRM4;
DT   14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT   14-OCT-2015, sequence version 1.
DT   24-JAN-2024, entry version 34.
DE   RecName: Full=peptidoglycan glycosyltransferase {ECO:0000256|ARBA:ARBA00012555};
DE            EC=2.4.1.129 {ECO:0000256|ARBA:ARBA00012555};
OS   Alloactinosynnema sp. L-07.
OC   Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC   Pseudonocardiaceae.
OX   NCBI_TaxID=1653480 {ECO:0000313|EMBL:CRK60641.1, ECO:0000313|Proteomes:UP000076116};
RN   [1] {ECO:0000313|Proteomes:UP000076116}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=L-07 {ECO:0000313|Proteomes:UP000076116};
RA   Ramaraj T.;
RL   Submitted (MAY-2015) 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; LN850107; CRK60641.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0H5CRM4; -.
DR   STRING; 1653480.gene:80949527; -.
DR   KEGG; alo:CRK60641; -.
DR   Proteomes; UP000076116; 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:SF34; 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   Glycosyltransferase {ECO:0000313|EMBL:CRK60641.1};
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   Reference proteome {ECO:0000313|Proteomes:UP000076116};
KW   Transferase {ECO:0000313|EMBL:CRK60641.1};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        61..81
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          108..279
FT                   /note="Glycosyl transferase family 51"
FT                   /evidence="ECO:0000259|Pfam:PF00912"
FT   DOMAIN          372..621
FT                   /note="Penicillin-binding protein transpeptidase"
FT                   /evidence="ECO:0000259|Pfam:PF00905"
FT   REGION          1..42
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          679..747
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        689..734
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   747 AA;  81093 MW;  48CAC8A46CB47EEE CRC64;
     MYLPQNPGQG RSEPALLTHR EPDYEDNYVD NDDYGPDEDP LTDAESKRLR RKKIWRRVRR
     TAYVGTALMI ILPVLAFFIT YQMVEVESPE QVANQQDKVV TLNWADGSEM AKLAKSGGNR
     IMLTYDQIPK HVLHAVYAAE DATFETNSGF DLGGIARAAW NNVTGGGGGG STISQQYIKK
     ASGDDDATLT RKWVEVVKSY KMNETFDKPE IITAYLNTIY FGRGAYGIAA AGKAYYGVDD
     LNLLSKSQAA LLAGMIQTPS RHKEAAYQMG RWEYVTGRMV ANGWMTETER AQQPFVPPVP
     LADTKGEGLP GPLTELPTLV YAELKDRGIT EEAIKRNGYK ITLTIDKTAQ DLAEKAVSEV
     MTGQPANLHP GLVAVDPKKG HIIAYYPSAN GIGTDWAAEP QEPGSSFKPF DLVGLLKKGK
     GLYETYDSSN RKIPPTAKQE VKNASKPGCG ECTVAQAMKE SLNVVFTDMV YKDVKVNGVI
     DAAKQAGVRS PLDAASSDLN IAIGGGRTQV STVDMASAYA TFAAGGIYRM PRLVSKVENP
     NGSIILDETT QAVYQEKNAF DENPDTNSKI ARNVTEALLP VPQYSHIECA SGRQCAGKTG
     THQYGETQHN SKAWMVGYTP QISAAVSLSG DSNELRLIDA KGKIIYGGGL PGKIWQKFMN
     SYHQTNKLKQ ENFGKFVPIG KVESKPPATA TAPPTTTTQP SNSTPPTTTT EKPTKTTDPD
     PTTTSRTRPT RPSVTTEPII PLPGNGG
//