ID D8JPH9_HYPDA Unreviewed; 701 AA.
AC D8JPH9;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, sequence version 1.
DT 18-JUN-2025, entry version 82.
DE RecName: Full=peptidoglycan glycosyltransferase {ECO:0000256|ARBA:ARBA00044770};
DE EC=2.4.99.28 {ECO:0000256|ARBA:ARBA00044770};
DE Flags: Precursor;
GN OrderedLocusNames=Hden_0043 {ECO:0000313|EMBL:ADJ21870.1};
OS Hyphomicrobium denitrificans (strain ATCC 51888 / DSM 1869 / NCIMB 11706 /
OS TK 0415).
OC Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
OC Hyphomicrobiales; Hyphomicrobiaceae; Hyphomicrobium.
OX NCBI_TaxID=582899 {ECO:0000313|EMBL:ADJ21870.1, ECO:0000313|Proteomes:UP000002033};
RN [1] {ECO:0000313|Proteomes:UP000002033}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51888 / DSM 1869 / NCIB 11706 / TK 0415
RC {ECO:0000313|Proteomes:UP000002033};
RX PubMed=21705585; DOI=10.1128/JB.05453-11;
RG US DOE Joint Genome Institute;
RA Brown P.J., Kysela D.T., Buechlein A., Hemmerich C., Brun Y.V.;
RT "Genome sequences of eight morphologically diverse alphaproteobacteria.";
RL J. Bacteriol. 193:4567-4568(2011).
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=2.4.99.28;
CC Evidence={ECO:0000256|ARBA:ARBA00049902};
CC -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC {ECO:0000256|ARBA:ARBA00004752}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the transpeptidase
CC family. {ECO:0000256|ARBA:ARBA00007090}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the
CC glycosyltransferase 51 family. {ECO:0000256|ARBA:ARBA00007739}.
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DR EMBL; CP002083; ADJ21870.1; -; Genomic_DNA.
DR RefSeq; WP_013214089.1; NC_014313.1.
DR AlphaFoldDB; D8JPH9; -.
DR STRING; 582899.Hden_0043; -.
DR CAZy; GT51; Glycosyltransferase Family 51.
DR KEGG; hdn:Hden_0043; -.
DR eggNOG; COG4953; Bacteria.
DR HOGENOM; CLU_006354_7_3_5; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000002033; Chromosome.
DR GO; GO:0030288; C:outer membrane-bounded periplasmic space; IEA:TreeGrafter.
DR GO; GO:0004180; F:carboxypeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:InterPro.
DR GO; GO:0008658; F:penicillin binding; IEA:InterPro.
DR GO; GO:0008955; F:peptidoglycan glycosyltransferase activity; IEA:InterPro.
DR GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-UniPathway.
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; IPR004827; bZIP.
DR InterPro; IPR001264; Glyco_trans_51.
DR InterPro; IPR050396; Glycosyltr_51/Transpeptidase.
DR InterPro; IPR023346; Lysozyme-like_dom_sf.
DR InterPro; IPR011815; PBP_1c.
DR InterPro; IPR009647; PBP_C.
DR InterPro; IPR036950; PBP_transglycosylase.
DR InterPro; IPR001460; PCN-bd_Tpept.
DR NCBIfam; TIGR02073; PBP_1c; 1.
DR PANTHER; PTHR32282; BINDING PROTEIN TRANSPEPTIDASE, PUTATIVE-RELATED; 1.
DR PANTHER; PTHR32282:SF15; PENICILLIN-BINDING PROTEIN 1C; 1.
DR Pfam; PF06832; BiPBP_C; 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.
DR PROSITE; PS00036; BZIP_BASIC; 1.
PE 3: Inferred from homology;
KW Carboxypeptidase {ECO:0000256|ARBA:ARBA00022645};
KW Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022670};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000002033};
KW Transferase {ECO:0000256|ARBA:ARBA00022676}.
FT DOMAIN 209..224
FT /note="BZIP"
FT /evidence="ECO:0000259|PROSITE:PS00036"
SQ SEQUENCE 701 AA; 76077 MW; AF823BE1B2C33ABE CRC64;
MTWRRLGLAI LLVALTGAAT TYGLYVKAFA DAGPLLLDEA KATSVTVVDR DERLLRAFTT
TAGNWRLPID PKDVDQHYLK MLFAFEDKRF YSHHGVDPKA VLRAVGQLLR HGRLVSGGST
LTMQVSRLLD GKHERTASGK LRQMARAINL ERKLSKTEIL KLYLRLAPFG GNLEGVRAAS
LAYFGKEPRR LSLGEAALLV ALPQSPEQRR LDRNPEAARR ARDRVLDRAV AAHVITAADA
ARAKTERVVK ARYAFPMLAP HLTETQVATH PKENILKLTL DRTLQASLEK LATEQARLIG
DKVSAAIVVA DHQTGEILAQ VGSAGYMDTG RQGAVDMSTA VRSPGSTLKP FIYGLAFEAG
LAHPETLIDD RATRFGTYAP KNFDENFHGT VSIREALEQS LNIPAVRVLA RVGPGKLVGR
FRRAGVDARF PDKSEPTLAM ALGGTGLTLE EMTQLYASLA RGGDSIALVH RLDERGRTLA
ATRVKPLVNA HRLMSPLAAW YVTDILKDAP PPPNAKGGRF AYKTGTSYGY RDAWAIGYDG
KYVVAAWVGK PDNSSVPGIL GRTAAAPILF DAFARISEKR AALQAMPANA IKGTNADLPA
PLKRWRDPSD DPATGRFLEP PVLISFPPDQ SEIEGAELGG DPLILKADGG ALPLTWLIDG
TPIESNPHSR EATWQPGTAG FAKLTVIDAK GRTDRASIRL R
//
