ID W0QD18_9PAST Unreviewed; 850 AA.
AC W0QD18;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 24-JAN-2024, entry version 45.
DE RecName: Full=Penicillin-binding protein 1A {ECO:0000256|ARBA:ARBA00018638};
DE EC=2.4.1.129 {ECO:0000256|ARBA:ARBA00012555};
DE EC=3.4.16.4 {ECO:0000256|ARBA:ARBA00012448};
GN ORFNames=X808_6150 {ECO:0000313|EMBL:AHG75138.1};
OS Mannheimia varigena USDA-ARS-USMARC-1296.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Mannheimia.
OX NCBI_TaxID=1433287 {ECO:0000313|EMBL:AHG75138.1, ECO:0000313|Proteomes:UP000066995};
RN [1] {ECO:0000313|EMBL:AHG75138.1, ECO:0000313|Proteomes:UP000066995}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=USDA-ARS-USMARC-1296 {ECO:0000313|EMBL:AHG75138.1,
RC ECO:0000313|Proteomes:UP000066995};
RA Harhay G.P., Clawson M.L., Murray R.W., Lubbers B.V., Heaton M.P.,
RA Chitko-Mckown C.G., Harhay D.M., Smith T.P.L.;
RT "Annotation of the Mannheimia varigena USDA-ARS-USMARC-1296 complete
RT genome.";
RL Submitted (DEC-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Cell wall formation. Synthesis of cross-linked peptidoglycan
CC from the lipid intermediates. The enzyme has a penicillin-insensitive
CC transglycosylase N-terminal domain (formation of linear glycan strands)
CC and a penicillin-sensitive transpeptidase C-terminal domain (cross-
CC linking of the peptide subunits). {ECO:0000256|ARBA:ARBA00002624}.
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 -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000256|ARBA:ARBA00004249}; Single-pass type II membrane protein
CC {ECO:0000256|ARBA:ARBA00004249}. Membrane
CC {ECO:0000256|ARBA:ARBA00004606}; Single-pass type II membrane protein
CC {ECO:0000256|ARBA:ARBA00004606}.
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; CP006943; AHG75138.1; -; Genomic_DNA.
DR RefSeq; WP_025216886.1; NZ_CP006943.1.
DR AlphaFoldDB; W0QD18; -.
DR STRING; 1433287.X808_6150; -.
DR KEGG; mvi:X808_6150; -.
DR PATRIC; fig|1433287.3.peg.611; -.
DR eggNOG; COG5009; Bacteria.
DR HOGENOM; CLU_006354_2_4_6; -.
DR OrthoDB; 9766909at2; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000066995; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0008658; F:penicillin binding; IEA:InterPro.
DR GO; GO:0008955; F:peptidoglycan glycosyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0009002; F:serine-type D-Ala-D-Ala carboxypeptidase 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 GO; GO:0046677; P:response to antibiotic; 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; IPR031376; PCB_OB.
DR InterPro; IPR001460; PCN-bd_Tpept.
DR NCBIfam; TIGR02074; PBP_1a_fam; 1.
DR PANTHER; PTHR32282; BINDING PROTEIN TRANSPEPTIDASE, PUTATIVE-RELATED; 1.
DR PANTHER; PTHR32282:SF27; PENICILLIN-BINDING PROTEIN 1A; 1.
DR Pfam; PF17092; PCB_OB; 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 Antibiotic resistance {ECO:0000256|ARBA:ARBA00023251};
KW Carboxypeptidase {ECO:0000256|ARBA:ARBA00022645};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Signal-anchor {ECO:0000256|ARBA:ARBA00022968};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022968}.
FT DOMAIN 55..227
FT /note="Glycosyl transferase family 51"
FT /evidence="ECO:0000259|Pfam:PF00912"
FT DOMAIN 315..407
FT /note="Penicillin-binding protein OB-like"
FT /evidence="ECO:0000259|Pfam:PF17092"
FT DOMAIN 412..587
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
SQ SEQUENCE 850 AA; 94025 MW; FDFB528E2529471F CRC64;
MRIAKIIFSA LFSLLILGGV IGGLLYMHIK SDLPDVATLK NVELQQPMQI FTLDGKLIGE
VGEERRIPVK LEDVPPMLVK AILATEDARF YEHKGIDPKG IMRAVWRTSQ GDTQGASTIT
QQLAKNFFLT PERSIERKAK EAILALEIEQ VLTKNEILEL YLNKIYLGYR SHGVAAAAKT
YFNKSLKDLT LSEIAIIAGL PKAPSTMNPL YSVKRAEDRR NVVLGRMLET KDITQKEYEK
AKAEPVVANY YGATLEFRAD YVTEMVRQEI VKRYGENIAY NKGLKVYATV LSHDQKAAQD
ALRENLIDYD RRRGWRGADK LWTGSSVWDD EKIIEHLSKL PKSDPFTPAV VMQTDKSKYT
LLLANGEPAT LKRVNASFAP KGLKVGEQIW VRLNKAKEWT LGQVPEVNSA LVSINSENGA
IEAIVGGFSF EQSRFNRATQ SLVQVGSAIK PFIYAAAMNK GLSLSTTISD GPIVIKKKGQ
KEWRPKNADG VYGGPTRARV ALGKSRNMVA IRVLQMAGID YTADYLQRFG FNRNQYIATE
SLALGAASFT PLEMARAYAV FNNGGYLIEP YIIDRIIDAQ GYELYQANPV VSCSVCDNPV
IYPEPKYFDS VKIHDETQVA TTPVTQNSTE EEVVEDIVES EPELQAENSE KNAPSLMAES
SHHVKGLRYA PHVISNELAF LMRSALATAV TGEPEYGWRG TSYRMLNTIK RADVGGKTGT
TNNSKATWYA GFGADIATVV YVGFDDNKRE LGKGASGSVT ALPAWVNYMK VALADKPVQK
DVVPGNIVEV KIDPNSGFLG NGRKEFFIKG TEPTKRYVVE RGYTEKSPTQ TVPARLGLPP
PGVLQSGELF
//
