ID A0A2P2BUC2_9FIRM Unreviewed; 926 AA.
AC A0A2P2BUC2;
DT 23-MAY-2018, integrated into UniProtKB/TrEMBL.
DT 23-MAY-2018, sequence version 1.
DT 27-MAR-2024, entry version 24.
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=FRIFI_2441 {ECO:0000313|EMBL:CEI73966.1};
OS Romboutsia hominis.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Peptostreptococcaceae;
OC Romboutsia.
OX NCBI_TaxID=1507512 {ECO:0000313|EMBL:CEI73966.1, ECO:0000313|Proteomes:UP000245695};
RN [1] {ECO:0000313|EMBL:CEI73966.1, ECO:0000313|Proteomes:UP000245695}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FRIFI {ECO:0000313|EMBL:CEI73966.1,
RC ECO:0000313|Proteomes:UP000245695};
RA Hornung B.V.;
RL Submitted (SEP-2014) 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 -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004401};
CC Single-pass type II membrane protein {ECO:0000256|ARBA:ARBA00004401}.
CC Membrane {ECO:0000256|ARBA:ARBA00004606}; Single-pass type II membrane
CC protein {ECO:0000256|ARBA:ARBA00004606}.
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DR EMBL; LN650648; CEI73966.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2P2BUC2; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000245695; Chromosome Chromosome1.
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; 2.
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; 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:SF33; PEPTIDOGLYCAN GLYCOSYLTRANSFERASE; 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 4: Predicted;
KW Antibiotic resistance {ECO:0000256|ARBA:ARBA00023251};
KW Carboxypeptidase {ECO:0000256|ARBA:ARBA00022645};
KW Glycosyltransferase {ECO:0000313|EMBL:CEI73966.1};
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:UP000245695};
KW Signal-anchor {ECO:0000256|ARBA:ARBA00022968};
KW Transferase {ECO:0000313|EMBL:CEI73966.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 63..87
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 116..272
FT /note="Glycosyl transferase family 51"
FT /evidence="ECO:0000259|Pfam:PF00912"
FT DOMAIN 458..723
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
FT REGION 1..55
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 800..926
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 17..46
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 826..926
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 926 AA; 99440 MW; 7B207338D3674070 CRC64;
MNNDNNENRN KIRRKKASSS SSTATRNSST TRSSSTSRGS STSSSNKKTK PKKKKDKFKT
LRSILVVCLV LLVAGVAVGT GVVFASLRNA EPISKALLEE KTYQTTRIYY ANNDLLSNAP
SVNKKQPVPL KDMGKYLPKA IVAIEDERFY EHGGVDIRGL LRSVVKTLTG DKQGGSTIPM
QVSKMLLTST EQSLPRKIKD IYYAHEMSKV LSKDEILELY LNNFFVGKGL AGAEAGARGY
FDKKASQLTL GESALLAGST QNPSRYSAYI TAKLEGNETK DDVANRLLFF INTPDDTLDD
PTPMELDMVE KLNSWGLIPN DDTYKQLKAG TMVVRKAVPN PKAKERRNIV LGKMLQTGAI
TQSEYNEAVA EEINIKLPKP KESVSSSVED LIEYKVIDAL VAQGNTKDEA YNMFYNGGLK
IHTTIDPKMQ KILEKEYDND NNFPGSRHSN GMTQPQSSMV ILDYKTGEIK ALVGGRHITG
RKTLNRATTP QQPGSTIKPL SVYTPAIDTL KLTQATALSD TTANLTPYKF KENNKWNPNT
TTPGKDIMSL RKALAYSSNT IAIRTAELLG DSYKDCVDIM MDYLKNFGIT TLVDSNTANA
ESNDRRFPAL TLGGMTHGIS PLEMASAYGT LANGGVYIEP TIFTTITSYD GQLIVKNTPE
QHKVVDPDVA YVITDMLKAV ITEGIGGKAA IPGGMPVAGK TGTTNKALDA WFVGYTPYYV
GATYIGDDAG RKNPTTGEFI PRESVEGGSG SAAKLWSIVM RQIHENLKKV DFKVPDKVYF
AKINLIDGGR SSSGVKAAFI DGTSPTKYTS RANAVKPKHE ESTTPPENQN NEGTVDNNTT
PPADNGGGNT TPPTDNGGGN TTPPADNGGG NTTPPADNGG GNTTTPPPNN GGGTATPPPS
NGGGNTTPPA DNSGGATNPA SNPTGQ
//
