ID A0A975K780_9SPHN Unreviewed; 708 AA.
AC A0A975K780;
DT 22-FEB-2023, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2023, sequence version 1.
DT 18-JUN-2025, entry version 12.
DE RecName: Full=peptidoglycan glycosyltransferase {ECO:0000256|ARBA:ARBA00044770};
DE EC=2.4.99.28 {ECO:0000256|ARBA:ARBA00044770};
GN Name=pbpC {ECO:0000313|EMBL:QUT06066.1};
GN ORFNames=KFK14_00750 {ECO:0000313|EMBL:QUT06066.1};
OS Sphingobium phenoxybenzoativorans.
OC Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
OC Sphingomonadales; Sphingomonadaceae; Sphingobium.
OX NCBI_TaxID=1592790 {ECO:0000313|EMBL:QUT06066.1, ECO:0000313|Proteomes:UP000681425};
RN [1] {ECO:0000313|EMBL:QUT06066.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Tas13 {ECO:0000313|EMBL:QUT06066.1};
RA Li Y.;
RT "Isolation of p-tert-butylphenol degrading bacteria Sphingobium
RT phenoxybenzoativorans Tas13 from active sludge.";
RL Submitted (APR-2021) 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=2.4.99.28;
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; CP073910; QUT06066.1; -; Genomic_DNA.
DR RefSeq; WP_212609522.1; NZ_CP073910.1.
DR KEGG; spph:KFK14_00750; -.
DR Proteomes; UP000681425; 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: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:InterPro.
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; 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.
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:UP000681425};
KW Transferase {ECO:0000256|ARBA:ARBA00022676}.
FT DOMAIN 68..227
FT /note="Glycosyl transferase family 51"
FT /evidence="ECO:0000259|Pfam:PF00912"
FT DOMAIN 305..572
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
FT DOMAIN 621..705
FT /note="Penicillin-binding C-terminal"
FT /evidence="ECO:0000259|Pfam:PF06832"
SQ SEQUENCE 708 AA; 76228 MW; ED39074B1C75A786 CRC64;
MIRRFLTIRH ALIAVGAVLL LALAALYFLT LPPALPAYDK VVADWHPSEA WLYDRDGRLI
DSERVDFRAR RLAWTPLDKV SPALVESVLN SEDRRFRYHD GIDWVAMGNA VRLRLTGGRS
RGASTISMQV AAFLAPDLAR PGARGWREKL RQMRAARALE ARWSKDEILA AYLNLAPFRG
EAQGIGAAAV SLFGKGADAL SRQDALMLTA LLPNPGARPE QVAARACRLG KLPDCSAMRA
AAASALSVAR SRALDPGLAP HLAAHLLTKP GMKVTTTIDA RLQRLAAVAL KRQLQGLGPD
RARDGAVVVV DNASGDVLAY VGGVGLGSTA AAVDGADAYR QAGSTLKPFL YAQVIERGWL
TAASILEDSP VQLDTASGLY VPQNYDRSFK GPVSVRSALA GSLNVPAVRA LLLDGVETFR
DRLWDLGYRG LTEDGSYYGF SLALGSAEVT LLEQANAYRT LANGGQWSPL RLRAEDGHDA
PRGIVSPQAA WIISDILSDA SARTRTFGVD SALRLPFWTA VKTGTSKAMR DNWCVGYSDR
FTVAVWVGNL EGDSMKAVSG TSGAAPVWRD VMLALHAGQP GQTPPRPDGM EQRRVAFQNS
IEPQRDEWFV KGTGQPALAF APEAARRPRI VNPVNGSVYA LDPDIPIDRQ RLGAEVTGLV
AGHRLLLDNR DLGEADARPQ ILAGPGAHRL ALADPSGRIV DQVRFVVR
//
