ID W5T771_9NOCA Unreviewed; 813 AA.
AC W5T771;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE SubName: Full=Putative penicillin-binding protein {ECO:0000313|EMBL:AHH15180.1};
GN ORFNames=NONO_c03660 {ECO:0000313|EMBL:AHH15180.1};
OS Nocardia nova SH22a.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC Nocardia.
OX NCBI_TaxID=1415166 {ECO:0000313|EMBL:AHH15180.1, ECO:0000313|Proteomes:UP000019150};
RN [1] {ECO:0000313|EMBL:AHH15180.1, ECO:0000313|Proteomes:UP000019150}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SH22a {ECO:0000313|EMBL:AHH15180.1};
RX PubMed=24747905;
RA Luo Q., Hiessl S., Poehlein A., Daniel R., Steinbuchel A.;
RT "Insights into the Microbial Degradation of Rubber and Gutta-Percha by
RT Analysis of the Complete Genome of Nocardia nova SH22a.";
RL Appl. Environ. Microbiol. 80:3895-3907(2014).
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; CP006850; AHH15180.1; -; Genomic_DNA.
DR AlphaFoldDB; W5T771; -.
DR STRING; 1415166.NONO_c03660; -.
DR KEGG; nno:NONO_c03660; -.
DR PATRIC; fig|1415166.3.peg.366; -.
DR eggNOG; COG0744; Bacteria.
DR HOGENOM; CLU_006354_2_6_11; -.
DR Proteomes; UP000019150; 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 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 Membrane {ECO:0000256|SAM:Phobius};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000019150};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 31..53
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 712..775
FT /note="PASTA"
FT /evidence="ECO:0000259|PROSITE:PS51178"
FT REGION 777..813
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 783..813
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 813 AA; 85181 MW; 5C8E562A4713B3A4 CRC64;
MTCPHGSPPT VHLACDSGPI RLGRVPISQT LARLAGACVL AAVLLAGLLF PLAGGFGYMS
NRAADAVDNV SSELVEGTAP AVSTMVDATG APIAWLYEQR RFEVPSDKIA NDMKLSIVSI
EDKRFAEHGG VDWQGTLRAF LTNTSSGEVQ QGASTIDQQY VKNFQLLVVA KTDAERRAAI
ETTPARKLRE IRMALTLEKE LTKDEILTRY LNLVPFGNGS YGIQDAAQTY FGVDAKDLKV
AQAAMLAGMV QSSSKLNPYT NPKGVTERRN TVLDTLIQNI PSRAEEFRAA KEQPLGVLPE
PKGLPRGCIA AQDRGYFCDY ALQYLANAGI SKDQIDKGGY LIRTTLDPNV QNSVKAAVNS
VTDPNLPDIA EVQSIIAPGQ DAHHILAMTS SRTYGLDQGA HETVQPQPYS MVGDGAGSIF
KIFTTAAAME KGLGTSAQLD VPSFYAAKGM GNGGAAGCPP ATYCVKNAGN YKSPESVTEA
LAQSPNTAFV KLIQDVGVTP TVDMAIRLGM RSYAEAGTSG HGNQSLGDMF KQQNLGSFTL
GPVAINPLEL SNVAATLASG GKWCPPSPIA EVLDRDGKQV PLTQQACEQV IDPGLANTLA
NALSEDAPHG TAAGSAHATG WNVPVSSKTG TTETHRSSAF LGFTNALAGA AYIYGDSPTP
GEICSFPLRS CGDGDLFGGN EPARSWFAGL KPVLDKYPPS VLPPLDDKYV RGSNNAQIPD
VNGMSESEAR SVLIGAGFQV STVTQPGSAA KGTVTATTPN GSAIPGSVIT VLVSDGTQRE
IPRPGPAAPP PGLPGLPGIP VPRLPPIPIP LPR
//
