ID Q5YN32_NOCFA Unreviewed; 812 AA.
AC Q5YN32;
DT 23-NOV-2004, integrated into UniProtKB/TrEMBL.
DT 23-NOV-2004, sequence version 1.
DT 27-MAR-2024, entry version 109.
DE RecName: Full=peptidoglycan glycosyltransferase {ECO:0000256|ARBA:ARBA00012555};
DE EC=2.4.1.129 {ECO:0000256|ARBA:ARBA00012555};
GN OrderedLocusNames=NFA_55570 {ECO:0000313|EMBL:BAD60409.1};
OS Nocardia farcinica (strain IFM 10152).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC Nocardia.
OX NCBI_TaxID=247156 {ECO:0000313|EMBL:BAD60409.1, ECO:0000313|Proteomes:UP000006820};
RN [1] {ECO:0000313|EMBL:BAD60409.1, ECO:0000313|Proteomes:UP000006820}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IFM 10152 {ECO:0000313|EMBL:BAD60409.1,
RC ECO:0000313|Proteomes:UP000006820};
RX PubMed=15466710; DOI=10.1073/pnas.0406410101;
RA Ishikawa J., Yamashita A., Mikami Y., Hoshino Y., Kurita H., Hotta K.,
RA Shiba T., Hattori M.;
RT "The complete genomic sequence of Nocardia farcinica IFM 10152.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:14925-14930(2004).
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; AP006618; BAD60409.1; -; Genomic_DNA.
DR AlphaFoldDB; Q5YN32; -.
DR STRING; 247156.NFA_55570; -.
DR CAZy; GT51; Glycosyltransferase Family 51.
DR KEGG; nfa:NFA_55570; -.
DR eggNOG; COG0744; Bacteria.
DR HOGENOM; CLU_006354_6_1_11; -.
DR OrthoDB; 9766909at2; -.
DR Proteomes; UP000006820; 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:UP000006820};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 84..104
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 132..305
FT /note="Glycosyl transferase family 51"
FT /evidence="ECO:0000259|Pfam:PF00912"
FT DOMAIN 398..656
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
FT REGION 1..76
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 692..712
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 743..812
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 748..770
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 812 AA; 84485 MW; FB663671D80AB574 CRC64;
MARRGGAATG PKPATARSAT GPRPAVDGAR RAGGATTGER RAASGPPSGP PPRRGGGSGG
SGGSGGGRGP GQGRRMPWRT IRRVMYVLTA LAIMVPSAVF LIAYTTVSVP QPGDLKTNQV
ATIYAQDGST VISKVVPPQG NRTEVTIDQI PPHVRNAVIA AEDRDFYTNP GFSISGFARA
ARDNVLGKES AGGGSTITQQ YVKNALVGDE RSLTRKMREL VISAKMARQW SKDEILAAYL
NTIYFGRGAY GIDAAAKAYF GKPVQELTVA EGAVLAATIQ LPSLLDPEKN PDGAKSRWNY
VLDGMVSGGN LSAAERQNMQ YPQVVSLAAN QDNELDSGPE GLIKTRVLEE LSAAGISEQQ
LNTAGLQITT TIDPQAQQAA VEAATAKMQG EPEQLRTAVV SIDPRTGAVR AYYGGTDGQG
YDFANAPLQT GSSFKVIGLA ANLEQGIPLS QMYDSSPLTV HGIKITNVEG ESCGMCTIAE
ALKRSLNTSF YRMQLDMQNG PQKIAEMGHR LGIPEELPGV GKTLSEPDGS GPNNGIVLGQ
YQARPLDMAS AYATLAASGV YHQPHFVQKV VTADGQVLLD RGEVPGEQRV SAAVADNVTA
AMKPIAAYSR NHGLAGGRES AAKTGTAQLL DTGENKDAWM VGYTPSLSTA VWVGSVDNSP
LRNYAGAMIY GSSLPSDIWK ATMDGALAGT PNETFPKPAP IKGQAGVPEW TAPYTPPSTT
EAPLLPPVVI TPTQVEILPG ITIPVPGVQP APQQTQQQRP QQNSESGPLP GQPVAPTGGA
SPGGGNGNGN GGGGGNADDE EGSDSPQPTR SR
//
