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Database: UniProt
Entry: A0A239BA33_9ACTN
LinkDB: A0A239BA33_9ACTN
Original site: A0A239BA33_9ACTN 
ID   A0A239BA33_9ACTN        Unreviewed;       700 AA.
AC   A0A239BA33;
DT   25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT   25-OCT-2017, sequence version 1.
DT   24-JAN-2024, entry version 22.
DE   RecName: Full=peptidoglycan glycosyltransferase {ECO:0000256|ARBA:ARBA00012555};
DE            EC=2.4.1.129 {ECO:0000256|ARBA:ARBA00012555};
GN   ORFNames=SAMN06264365_10971 {ECO:0000313|EMBL:SNS04806.1};
OS   Actinoplanes regularis.
OC   Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC   Micromonosporaceae; Actinoplanes.
OX   NCBI_TaxID=52697 {ECO:0000313|EMBL:SNS04806.1, ECO:0000313|Proteomes:UP000198415};
RN   [1] {ECO:0000313|EMBL:SNS04806.1, ECO:0000313|Proteomes:UP000198415}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 43151 {ECO:0000313|EMBL:SNS04806.1,
RC   ECO:0000313|Proteomes:UP000198415};
RA   Kim H.J., Triplett B.A.;
RL   Submitted (JUN-2017) 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; FZNR01000009; SNS04806.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A239BA33; -.
DR   Proteomes; UP000198415; Unassembled WGS sequence.
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; PENICILLIN-INSENSITIVE TRANSGLYCOSYLASE; 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:SNS04806.1}; Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW   Protease {ECO:0000256|ARBA:ARBA00022670};
KW   Reference proteome {ECO:0000313|Proteomes:UP000198415}.
FT   DOMAIN          61..244
FT                   /note="Glycosyl transferase family 51"
FT                   /evidence="ECO:0000259|Pfam:PF00912"
FT   DOMAIN          350..660
FT                   /note="Penicillin-binding protein transpeptidase"
FT                   /evidence="ECO:0000259|Pfam:PF00905"
FT   REGION          371..390
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        371..387
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   700 AA;  76122 MW;  9860FD81E06B3BE5 CRC64;
     MIRAGLIAGL VAAGLFYPFT ALAGMGVKAG ADALERMPEQ LTEAPAAQTT YVYAKDGKTL
     LTMFYEEYRR QVALKDMSPY ITQAIVASED TRFYEHHGVD AKGVARAFVA NQQAGGVSQG
     ASTLTMQYVR MALRDSAKTP REALEATEQT ATRKLREMRL AIEVEHRLSK QEILERYLNA
     AYFGHRAYGI HAAAGVFFSK APKNLTLTEA ALLAGLVKAP SAYDPATTDQ DAALQRRNYV
     IDQMLKMGSI TPAQAASAKK ARIRLKLSTP PNDCVSVPAE HNDWGFFCDY LKNWWREQPA
     FGESALEREE NLRRGGYRVI TSIDPAIQAS AVEHVLDKES KDSPFAHGEV VIQPGTGRVL
     SMAVNRTYSL HQEHNGKHSD RSQRDDIRGN YPNTVNPLLG GGDMAGYQAG STFKIFTLLA
     ALDAGLPLRT SYYAPERFVS KYITEPGPAT CGKHWCPKNS SKSMTGQQSM WSGFGKSVNT
     YFVQLEQRVG AEKAVAMAEK LGLKWRTPID KELARPANAA GWGAFTLGVS DATPVEIANV
     FATVAAEGTY CEALPVLSIR DSTGKNAMYR GRFVAAPRCH RVFSPEVARA ATDAARCVTG
     YGSARGGCGG WGTSEMVYGV VGRPVAGKSG TTDNNRTAWF SGFTPQLAAS AFVADPDNPK
     HYVGNGRSTI SKYTVAQTLR DALEGQPELK FTPPSDKLVW
//
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