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Database: UniProt
Entry: A0A143QE36_9NOCA
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Original site: A0A143QE36_9NOCA 
ID   A0A143QE36_9NOCA        Unreviewed;       949 AA.
AC   A0A143QE36;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   24-JAN-2024, entry version 32.
DE   RecName: Full=peptidoglycan glycosyltransferase {ECO:0000256|ARBA:ARBA00012555};
DE            EC=2.4.1.129 {ECO:0000256|ARBA:ARBA00012555};
GN   Name=ponA1 {ECO:0000313|EMBL:AMY21169.1};
GN   ORFNames=A3Q40_03821 {ECO:0000313|EMBL:AMY21169.1};
OS   Rhodococcus sp. PBTS 1.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC   Rhodococcus.
OX   NCBI_TaxID=1653478 {ECO:0000313|EMBL:AMY21169.1, ECO:0000313|Proteomes:UP000076180};
RN   [1] {ECO:0000313|EMBL:AMY21169.1, ECO:0000313|Proteomes:UP000076180}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PBTS 1 {ECO:0000313|EMBL:AMY21169.1,
RC   ECO:0000313|Proteomes:UP000076180};
RX   PubMed=27284129;
RA   Stamler R.A., Vereecke D., Zhang Y., Schilkey F., Devitt N., Randall J.J.;
RT   "Complete Genome and Plasmid Sequences for Rhodococcus fascians D188 and
RT   Draft Sequences for Rhodococcus Isolates PBTS 1 and PBTS 2.";
RL   Genome Announc. 4:0-0(2016).
RN   [2] {ECO:0000313|Proteomes:UP000076180}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PBTS 1 {ECO:0000313|Proteomes:UP000076180};
RA   Stamer R., Vereecke D., Zhang Y., Schilkey F., Devitt N., Randall J.;
RT   "Complete Genome and Plasmid Sequences for Rhodococcus fascians D188 and
RT   Draft Sequences for Rhodococcus spp. Isolates PBTS 1 and PBTS 2.";
RL   Submitted (APR-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; CP015219; AMY21169.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A143QE36; -.
DR   STRING; 1653478.A3Q40_03821; -.
DR   KEGG; rhu:A3Q40_03821; -.
DR   PATRIC; fig|1653478.3.peg.3879; -.
DR   Proteomes; UP000076180; 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   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   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:UP000076180};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        218..240
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          272..439
FT                   /note="Glycosyl transferase family 51"
FT                   /evidence="ECO:0000259|Pfam:PF00912"
FT   DOMAIN          535..788
FT                   /note="Penicillin-binding protein transpeptidase"
FT                   /evidence="ECO:0000259|Pfam:PF00905"
FT   REGION          1..211
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          744..764
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          824..874
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          898..949
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        12..46
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        71..92
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        159..185
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        192..208
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   949 AA;  97767 MW;  8F53295A34BF7E07 CRC64;
     MTTPYDGSRD DGAGAGNDRP RSDGPGYDDR YRDDRDDYRP RHQLPDDQPP RPPMPPRRGD
     GPGQYRGSYG PPPQGRPPQG PPQGPPPQYR APRPAYGTGE TPPRYDDGYR ARPAGPPRGP
     RRYDDTGYIA GAGAVGGAGA AGAAYSQARP PRDDAPTSGY GRGEYDRDDR APSGRDDRAA
     SGRDEDSSRS GGGPTEPPSG GRTTKTAKKS PWRTVRRTAY ALVALGLIVP ILAFMVAYVI
     EDVPRPGDIK TNQVATILAS DGTSVLGTVV PPEGNRTDVE IGQIPEHVRN AVLSAEDRDF
     YSNPGFSVSG FARAARDNVL GRDSAGGGST ITQQYVKNAL VGSERTLTRK MRELVISSKM
     ARQWTKDDIL AAYLNTIYFG RGAYGIAAAS KAYFDKPVEA LSVEEGAVLA AIIQQPSGLD
     PENNPVGAQS RWNYVLDGMV TMGALDQGAR SAMQYPATRP LASVNSGDAT DAGPNGLIKT
     QVLRELSSSG ISEQDLNTAG LQITTTIDPQ DQQAAIDAVN SNMEGEPSEL RTASVSIDPR
     TGAVKSYYGG ADGRGFDFAQ SGLQTGSSFK VFGLAAALDQ GIPLSQMYDS SPLTVNGISI
     GNVEGESCGT CTIAEALKRS LNTSFYRLQL GLDGGPQAVA DMAHRLGIPE EVEGIGPTLT
     EPNGAGPNNG IILGQYQSRV IDMASAYATL AASGTYHAPH FVQRVVTADG TVLLDRGTEP
     GEQRVDPNVA DNVTAAMRPI AGYSNGHNLA GGRPSAAKTG TAQLGDTGEN KDAWMVGYTP
     SLATAVWVGT EQGLPLRNVY GGPIYGSGLP SDIWKDTLDG SLEGTEVESF PAPGAIAGQA
     GVPQYSAPAP TRAPVATTSE APSAPPTTEA PPPQVVVPSQ VEILPGITIP VPGLAPAATT
     TAPGAEPGAG AGGGTGAGEG TGGGAGAGAG AEGGAGAGAG QPPAASPGG
//
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