ID A0A148NBE0_9GAMM Unreviewed; 778 AA.
AC A0A148NBE0;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 24-JAN-2024, entry version 32.
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=AXA67_03475 {ECO:0000313|EMBL:KXJ41867.1};
OS Methylothermaceae bacteria B42.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Methylococcales;
OC Methylothermaceae.
OX NCBI_TaxID=1798802 {ECO:0000313|EMBL:KXJ41867.1, ECO:0000313|Proteomes:UP000074680};
RN [1] {ECO:0000313|EMBL:KXJ41867.1, ECO:0000313|Proteomes:UP000074680}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B42 {ECO:0000313|EMBL:KXJ41867.1};
RX PubMed=26779119; DOI=10.3389/fmicb.2015.01425;
RA Skennerton C.T., Ward L.M., Michel A., Metcalfe K., Valiente C., Mullin S.,
RA Chan K.Y., Gradinaru V., Orphan V.J.;
RT "Genomic Reconstruction of an Uncultured Hydrothermal Vent
RT Gammaproteobacterial Methanotroph (Family Methylothermaceae) Indicates
RT Multiple Adaptations to Oxygen Limitation.";
RL Front. Microbiol. 6:1425-1425(2015).
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}.
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:KXJ41867.1}.
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DR EMBL; LSNW01000005; KXJ41867.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A148NBE0; -.
DR STRING; 1798802.AXA67_03475; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000074680; Unassembled WGS sequence.
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..230
FT /note="Glycosyl transferase family 51"
FT /evidence="ECO:0000259|Pfam:PF00912"
FT DOMAIN 317..425
FT /note="Penicillin-binding protein OB-like"
FT /evidence="ECO:0000259|Pfam:PF17092"
FT DOMAIN 427..673
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
FT REGION 757..778
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 759..778
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 778 AA; 86897 MW; 75883D360B56AE0B CRC64;
MRGLLKGFVW FLLLLLLLGG ALLGGVYYLY NPQLPNPDQL REVKYQLPLE IYSHDGQLIA
QFGDKKRTPL DIKQIPKPMI DAVLAAEDAR FYQHNGVDIQ GILRAAIELI RSGQKRQGGS
TITMQVARNF FLSPEKTYER KIKEILLALK IERHLSKDEI LELYLNKIYL GHHAYGVAAA
ANVYYGKDLA ELNLAQYAMI AGLPKAPSRY NPITNPSRAL ERRNYILKHM LEHGMIEVRE
YNQAIAQPVT ANLHKPKETL LASHLAEMVR QDLFERYGEA IYSEGYRVFT TLNLQLQKAA
DLAVKKGLHQ YDERHGYRGP EGKLPLNTPI EQVTQSLAKM GTKGLTTPGW VTSINPRANS
ANVLLEQDKT ITLTWENIRW ARPALANNHL GKPPTSVTQV LKPGDLIRVR FTKDGQWRLT
QIPKVEGALV SVDSRTGAII ALVGGYDFAL SKFNRVTDAQ RQPGSGFKPV LYTAALESGF
TAASLFNDAP IVYTDSEGDW RPQNYSGRFY GPTRLRVALR NSRNLVSIRL LQEVGLDKVI
EVARRFGFKP EQLPKSPTLA LGSGTATPLD MARMFSVFAN GGYRINPYYI ERIETADGTV
IEQSQPKRAC NQCLDSAPRI LAPRIHYIMH SLLQDVVRRG TAVKAKVLKR SDLAGKTGTT
NDQRDAWFNG YASPLVAVSW VGFDSAKPLG NGETGGKAAL PIWIEYMKTA LKDQPENAFP
MPKGIVTVPI NPETGLRVTS NAHAIHEIFR EEFAPEEETA NFQNDSQQPQ DSVLNSLF
//
