ID A0A558NHJ1_9GAMM Unreviewed; 805 AA.
AC A0A558NHJ1;
DT 16-OCT-2019, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2019, sequence version 1.
DT 18-JUN-2025, entry version 26.
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:TVV42078.1};
GN ORFNames=FOT50_15895 {ECO:0000313|EMBL:TVV42078.1};
OS Thalassolituus sp. C2-1.
OC Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
OC Oceanospirillales; Oceanospirillaceae; Thalassolituus.
OX NCBI_TaxID=2597518 {ECO:0000313|EMBL:TVV42078.1, ECO:0000313|Proteomes:UP000316365};
RN [1] {ECO:0000313|EMBL:TVV42078.1, ECO:0000313|Proteomes:UP000316365}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C2-1 {ECO:0000313|EMBL:TVV42078.1,
RC ECO:0000313|Proteomes:UP000316365};
RA Wei Y.;
RT "Thalassolituus sedimis sp. nov., isolated from a deep-sea sediment of
RT Mariana Trench.";
RL Submitted (JUL-2019) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:TVV42078.1}.
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DR EMBL; VNIL01000006; TVV42078.1; -; Genomic_DNA.
DR RefSeq; WP_145470048.1; NZ_CP094879.1.
DR AlphaFoldDB; A0A558NHJ1; -.
DR OrthoDB; 9766909at2; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000316365; Unassembled WGS sequence.
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: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; 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:UP000316365};
KW Transferase {ECO:0000256|ARBA:ARBA00022676}.
FT DOMAIN 82..248
FT /note="Glycosyl transferase family 51"
FT /evidence="ECO:0000259|Pfam:PF00912"
FT DOMAIN 325..557
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
FT DOMAIN 718..799
FT /note="Penicillin-binding C-terminal"
FT /evidence="ECO:0000259|Pfam:PF06832"
SQ SEQUENCE 805 AA; 89970 MW; 617528B30265CC07 CRC64;
MSNPPANRAA FNAARFFRLP QNRAARFLLW LVFFCLLLKS ADWLWPLAVP DPQRQTEGAQ
NDFAQLVVDR HERPLRAFAD SNGVWRYPVE LNEVSPFYKD ALLNYEDRWF YYHPGINPFA
LLRAAWQNWR CGCVVSGGST ISMQVARRFH PHSRSVGGKL EQALRALQLE WHYSKDEIFT
LYLNYAPMGG VIEGVGAASR LYLDKPALDL SLAESALMAV LPQAPSRLRP DRYPQRALNA
RNKVLQRMLE FGVITATDYQ QALLEPVLAY QPHTPQLAPL LARELRRQNA DKSLIKTTLD
ADLQYEIEDY LAQEIQRFPP SHSAAILVLD NASHEVRAYA GSADFADDSR FGHVDMVQAQ
RSPGSTLKPF IYGLAIEDGL IHSASLLRDV PRYFTDYQPE NFTRHFSGPV SATEALRQSL
NLPVVQVLEA VTPERFAAAL ANAGARYRIP GDGKANLSMA LGGGGLSLAQ LVQLYSSIAN
QGQVWPLRYL TEESPSAAGS RWLFSAETAW VLNDMLRSPR PDRARSYALQ DNDRSIAWKT
GTSYGFRDAW AVGVTPAYTI GVWFGRPDGT PSPGHYGALS ALPVLFQLFD RIEHKPELLP
QPEQVSQETI CWPLGKSAAE TPADQCFQTH KAWLVRRQLP PTLRDERSDG LWRNPLTYWT
SERGLLVDGS CDVPARTAHQ LALWPRPLEH WLPASQRLRN RLPAVDPRCS EPPALALEPL
QITGIQDGLI LRSSRTRAGG SAALPEISLH AQGGLGQRDW YVNGLHVGSS GEAETLSYRF
SVTGEQEVVV MDAQGELDRR TLQVE
//
