ID A6H1R6_FLAPJ Unreviewed; 791 AA.
AC A6H1R6;
DT 24-JUL-2007, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2007, sequence version 1.
DT 18-JUN-2025, entry version 95.
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:CAL44290.1};
GN OrderedLocusNames=FP2234 {ECO:0000313|EMBL:CAL44290.1};
OS Flavobacterium psychrophilum (strain ATCC 49511 / DSM 21280 / CIP 103535 /
OS JIP02/86).
OC Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Flavobacterium.
OX NCBI_TaxID=402612 {ECO:0000313|EMBL:CAL44290.1, ECO:0000313|Proteomes:UP000006394};
RN [1] {ECO:0000313|EMBL:CAL44290.1, ECO:0000313|Proteomes:UP000006394}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49511 / DSM 21280 / CIP 103535 / JIP02/86
RC {ECO:0000313|Proteomes:UP000006394};
RX PubMed=17592475; DOI=10.1038/nbt1313;
RA Duchaud E., Boussaha M., Loux V., Bernardet J.F., Michel C., Kerouault B.,
RA Mondot S., Nicolas P., Bossy R., Caron C., Bessieres P., Gibrat J.F.,
RA Claverol S., Dumetz F., Le Henaff M., Benmansour A.;
RT "Complete genome sequence of the fish pathogen Flavobacterium
RT psychrophilum.";
RL Nat. Biotechnol. 25:763-769(2007).
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; AM398681; CAL44290.1; -; Genomic_DNA.
DR RefSeq; WP_011964324.1; NC_009613.3.
DR RefSeq; YP_001297091.1; NC_009613.3.
DR AlphaFoldDB; A6H1R6; -.
DR STRING; 402612.FP2234; -.
DR CAZy; GT51; Glycosyltransferase Family 51.
DR EnsemblBacteria; CAL44290; CAL44290; FP2234.
DR GeneID; 66553338; -.
DR KEGG; fps:FP2234; -.
DR PATRIC; fig|402612.5.peg.2284; -.
DR eggNOG; COG4953; Bacteria.
DR HOGENOM; CLU_006354_7_2_10; -.
DR OrthoDB; 9766909at2; -.
DR Proteomes; UP000006394; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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 ECO:0000313|EMBL:CAL44290.1};
KW Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676,
KW ECO:0000313|EMBL:CAL44290.1}; Hydrolase {ECO:0000256|ARBA:ARBA00022670};
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:UP000006394};
KW Transferase {ECO:0000313|EMBL:CAL44290.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 21..37
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 71..230
FT /note="Glycosyl transferase family 51"
FT /evidence="ECO:0000259|Pfam:PF00912"
FT DOMAIN 309..568
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
FT DOMAIN 697..784
FT /note="Penicillin-binding C-terminal"
FT /evidence="ECO:0000259|Pfam:PF06832"
SQ SEQUENCE 791 AA; 90235 MW; 544242CB59969314 CRC64;
MKAKITAFLQ RIINTIKRNK IKSSIAFILL MVYYFSLPST LFQEPYSTVI ESKEGELLGA
KIAHDGQWRF PAQDSVPYKF KKCIVYFEDE YFYKHPGFNP VAMVNAIKQN RKAGKVVRGG
STLTQQVIRL SRKGKNRTYF EKVIEIILAT RLELRHCKDK ILELYAAHAP FGGNVVGLEM
ASWRYFGVQS HQLSWAESAT LAVLPNAPSL IYPGKNQQKL LKKRNNLLLK LKIEGIIDAQ
TYELAIEEPL PQKPYDLPQI APHLLQRVAK NKEGTRLKTT VDIALQNRIN QIAKYYYNQY
KQNEVNNLAI IVIDIKTRNI ISYVGNSPTD LNHQKDVDII EAPRSTGSIL KPLLYAEMLD
EGELLPNTLV ADIPTQISGY TPQNFNLTFD GAVPAHRALS RSLNIPSVLM LQDFGVNKFY
EELQRFKLRD ISKSPDHYGL SLILGGAESN LWDLCRTYAG LSSTIDYFNK NNGNYRTKEF
VELNYDHNFT PDFGYDSKQK TILGAGAIWQ TYNAMEEVNR PEGDEAWKFY DSSLKIAWKT
GTSFGNRDAW AIGTNARYVV GVWVGNASGE GRPTLTGVTS AAPILFDVFN LLPRQKWFGM
PLLDLTEVEV CKLSGHLAQE DCPKIKQLVS LKGKTTSICP YHKTVHLDKT GKYRVNSSCE
NVENIMTKKW FVLPPVMEWY YKNQHVDYLP LPPYRSDCAG TLTPSMDFIY PKTNSKIYLT
KNFNSEIQPV ILKIAHSNRE TEVYWYIDNV YKGSTKTFHE MAITPTQGFH YITVIDESGY
EIRKKIEIVR D
//
