ID A0A1Q4YRB4_9PSEU Unreviewed; 823 AA.
AC A0A1Q4YRB4;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=Penicillin-binding protein {ECO:0000313|EMBL:OKI37120.1};
GN ORFNames=A6A25_19005 {ECO:0000313|EMBL:OKI37120.1};
OS Saccharothrix sp. CB00851.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Saccharothrix.
OX NCBI_TaxID=1835005 {ECO:0000313|EMBL:OKI37120.1, ECO:0000313|Proteomes:UP000186828};
RN [1] {ECO:0000313|EMBL:OKI37120.1, ECO:0000313|Proteomes:UP000186828}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CB00851 {ECO:0000313|EMBL:OKI37120.1,
RC ECO:0000313|Proteomes:UP000186828};
RX PubMed=27999165; DOI=10.1128/mbio.02104-16;
RA Yan X., Ge H., Huang T., Hindra, Yang D., Teng Q., Crnovcic I., Li X.,
RA Rudolf J.D., Lohman J.R., Gansemans Y., Zhu X., Huang Y., Zhao L.X.,
RA Jiang Y., Van Nieuwerburgh F., Rader C., Duan Y., Shen B.;
RT "Strain Prioritization and Genome Mining for Enediyne Natural Products.";
RL MBio 7:e02104-e02116(2016).
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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OKI37120.1}.
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DR EMBL; LWLC01000004; OKI37120.1; -; Genomic_DNA.
DR RefSeq; WP_073886833.1; NZ_LWLC01000004.1.
DR AlphaFoldDB; A0A1Q4YRB4; -.
DR STRING; 1835005.A6A25_19005; -.
DR Proteomes; UP000186828; 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 CDD; cd06577; PASTA_pknB; 1.
DR Gene3D; 3.30.10.20; -; 1.
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; IPR005543; PASTA_dom.
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; PF03793; PASTA; 1.
DR Pfam; PF00912; Transgly; 1.
DR Pfam; PF00905; Transpeptidase; 1.
DR SMART; SM00740; PASTA; 1.
DR SUPFAM; SSF56601; beta-lactamase/transpeptidase-like; 1.
DR SUPFAM; SSF53955; Lysozyme-like; 1.
DR PROSITE; PS51178; PASTA; 1.
PE 4: Predicted;
KW Carboxypeptidase {ECO:0000256|ARBA:ARBA00022645};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000186828}.
FT DOMAIN 711..774
FT /note="PASTA"
FT /evidence="ECO:0000259|PROSITE:PS51178"
FT REGION 740..761
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 774..823
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 778..823
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 823 AA; 88117 MW; 8BFFF94648BDB124 CRC64;
MRARNGVLKL LGLCLLAGVL LAGMLFPVVG SLGMVSNRAS DTVDSISADL VTTDPPLIST
ITDKDGAPIA YLYDQYRVLV PPEMISPTMK AALVSVEDRR FYEHQGVDWR GTIRAGLTNQ
FSGSVTQGAS TLTQQYVKNY LVHVVARNNQ VEQQKAQEQT VARKAREWRI SLQLESQLGK
EEILARYLNV VPFGSTIYGI AAASQAYFNT TADKLTVSQA AMLAGMVNSP SALNPEVFPE
KALERRNQVI DKMVENDKLS RDAAEAAKAE PLGLATPVRT PANGCIGAGP EHGFFCSYAL
TYLERNGFSL EQLKTGGYTI RTTLDRTITD HAKRAAEAQV AKSTDGIANT MAVVRPGKER
HEVVALVANR DYGLKADQFQ TQFDLPSGVE NKFGAGSVYK VFTAAAALEK GMGIENTMAT
PNSYVSRVFK GGGDKCPPAP EPATRWYCLG NASSNYPPQM SLQTALQTSP NTGFVILEEQ
LGMDPVVDMA SRLGMRETMA TNIAGVRPDP KAKNKELRIS QTEFYKSNGG NASFTLSPAP
VSTLELANVA ATIMSGGVWC PPSPINQILD RNGKPVPVNE APCEQVVAEP LANGLAVGMS
KDDQGAGTAA RAAQQFKWTR PMLGKTGTTE DYKSAAFIGA TPDFAGAVQT FNDGVEPRGI
CVNGGPPRLC AKGDIYGGTV PARTWFETMT KIHEGLPVRG MPPVEERYLK GGSEIRIPDV
VGRNINDATR ILEQAGYKVS AQNRNSEQPK GQVVSQTPRG SALKGTIVTL LVSTGYVPPP
QPSDPPPTTE SPDPGQGNPG RPTGPGRPTG PPQITLPTDP PRR
//
