ID A0A345YFH7_9SPHN Unreviewed; 832 AA.
AC A0A345YFH7;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=Penicillin-binding protein {ECO:0000313|EMBL:AXK42679.1};
GN ORFNames=DVR09_10355 {ECO:0000313|EMBL:AXK42679.1};
OS Erythrobacter aureus.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Erythrobacteraceae; Erythrobacter/Porphyrobacter group; Erythrobacter.
OX NCBI_TaxID=2182384 {ECO:0000313|EMBL:AXK42679.1, ECO:0000313|Proteomes:UP000254508};
RN [1] {ECO:0000313|Proteomes:UP000254508}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YH-07 {ECO:0000313|Proteomes:UP000254508};
RA Tang T., Liu Q., Sun X.;
RT "Genome sequence of Erythrobacter strain YH-07, an antagonistic bacterium
RT isolated from Yellow Sea.";
RL Submitted (JUL-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Preferential cleavage: (Ac)2-L-Lys-D-Ala-|-D-Ala. Also
CC transpeptidation of peptidyl-alanyl moieties that are N-acyl
CC substituents of D-alanine.; EC=3.4.16.4;
CC Evidence={ECO:0000256|ARBA:ARBA00034000};
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};
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; CP031357; AXK42679.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A345YFH7; -.
DR KEGG; err:DVR09_10355; -.
DR OrthoDB; 9766909at2; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000254508; 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: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; 2.
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:SF27; 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 3: Inferred from homology;
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:UP000254508};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 37..56
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 82..259
FT /note="Glycosyl transferase family 51"
FT /evidence="ECO:0000259|Pfam:PF00912"
FT DOMAIN 436..693
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
FT REGION 803..832
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 832 AA; 91386 MW; 7B8B6B3DAEB62B4F CRC64;
MSDEPSLTYY RYRISRDPKR LVAWFTDNWA HNRKLRAASY IGGFAVVTLV LAWATLGRNL
PDAESLLEYE TPLPTVVRGI DGEIVHTYAR ERRVQLQYVD FPERLIEAYL SAEDKTFFSH
GGVDITGTAN AVIDYATKFG SGERAVGGST ITQQVAKNLL LGDEYSVTRK LKEMILATRI
ESVLTKQEIL ELYLNEIPLG RRSFGVQAAA RAYFDKDVGD LDLHEMAFLA ILPKAPERYG
RERHRDLALV RRNFVLDQMV ANGFIGADEG AAAKRLDLGL VRQRSERSAD AGYFLEEVRR
QLIEKFGETA DDGRNSVYSG GLWVRTSLDT ELQDAARDAL RAQLLSYHGN RGFTGPIATL
NPDNGDLTAQ LASSNISINY EDWRIGVVTA PGRVGFTDGE EHPLSGGPST LKAGDVVATV
KSGNGYAIRG VPEVSGAFLA EAPQTGRILA MQGGFDSRLG SFNRATQALR QPGSTIKPFV
YAAALDQGMT PATQVPDQTF CVWQGANLGE KCFRNFGGGG GGVHTMRWGL EQSRNLMTVH
IADDAGMDNV IKTIARLGIG EYEPYYSFAL GAGDTTVARM VNAYAALANW GRQNEGSVID
YVQDRDGKVI FRTDTRDCSG CNMEEWDGQP MPRFDVSGRQ VMDPRTAFQM VHMLQGVVTR
GTAVRLRSLD LPLFGKTGTT NGPTNAWFVG GSPEIIAGMY VGFDQPRNLG GWVQGGNTAA
TIMKRFVDAT KDRWTAEDFI APPGIRMVKI DRRSGKRVFD GRPSDEPTAA IIWEAFKPDT
EPPRSTRSDA IAAKRNEILE LIRRGRQGAT SAANSGRDDE PSDFVEDQGG IY
//
