ID A0A099CT87_9GAMM Unreviewed; 842 AA.
AC A0A099CT87;
DT 07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 1.
DT 24-JAN-2024, entry version 40.
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=HNQ86_002652 {ECO:0000313|EMBL:MBB6185307.1}, LF63_0112995
GN {ECO:0000313|EMBL:KGI76842.1};
OS Oleiagrimonas soli.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Rhodanobacteraceae; Oleiagrimonas.
OX NCBI_TaxID=1543381 {ECO:0000313|EMBL:KGI76842.1, ECO:0000313|Proteomes:UP000029708};
RN [1] {ECO:0000313|EMBL:KGI76842.1, ECO:0000313|Proteomes:UP000029708}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=3.5X {ECO:0000313|EMBL:KGI76842.1,
RC ECO:0000313|Proteomes:UP000029708};
RA Fang T., Wang H.;
RT "Xanthomonadaceae 3.5X direct submission.";
RL Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:MBB6185307.1, ECO:0000313|Proteomes:UP000560000}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 107085 {ECO:0000313|EMBL:MBB6185307.1,
RC ECO:0000313|Proteomes:UP000560000};
RA Goeker M.;
RT "Genomic Encyclopedia of Type Strains, Phase IV (KMG-IV): sequencing the
RT most valuable type-strain genomes for metagenomic binning, comparative
RT biology and taxonomic classification.";
RL Submitted (AUG-2020) 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}.
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:KGI76842.1}.
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DR EMBL; JROI01000015; KGI76842.1; -; Genomic_DNA.
DR EMBL; JACHET010000001; MBB6185307.1; -; Genomic_DNA.
DR RefSeq; WP_043102442.1; NZ_KN196470.1.
DR AlphaFoldDB; A0A099CT87; -.
DR STRING; 1543381.LF63_0112995; -.
DR HOGENOM; CLU_006354_2_4_6; -.
DR OrthoDB; 9766909at2; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000029708; Unassembled WGS sequence.
DR Proteomes; UP000560000; 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 Glycosyltransferase {ECO:0000313|EMBL:MBB6185307.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:MBB6185307.1};
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:UP000029708};
KW Signal-anchor {ECO:0000256|ARBA:ARBA00022968};
KW Transferase {ECO:0000313|EMBL:MBB6185307.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..33
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 58..234
FT /note="Glycosyl transferase family 51"
FT /evidence="ECO:0000259|Pfam:PF00912"
FT DOMAIN 321..428
FT /note="Penicillin-binding protein OB-like"
FT /evidence="ECO:0000259|Pfam:PF17092"
FT DOMAIN 434..615
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
SQ SEQUENCE 842 AA; 91951 MW; DA32E288E3305644 CRC64;
MPIIKRLLRY ALILALAGTL LGAIAIGVAY WLISPRLPSV DSLKDVQMQV PLRVLSADGK
LIAEFGEMRR LPVKIDNVPA RLKHAVLAAE DDDFYHHGGV DWTGTLRAAI HVVLSGGKKT
QGGSTITQQV ARNFFLSSQK TYTRKITEIF TAFRIEHELT KDEILQLYLN KMFLGHRTYG
VGAAAQYYYG KTLDQLTIAE CAMIASTFQR PSVVNPTDHQ RLGHARRDYV LGRMLANNFI
TKAQYEEALA TPLHAAPHEL PIAAHAPYLA EMVRQAALDK LGNAALTDGY VIHTTIRAQD
QADAVAAVRK GLLEYDRRHG YRGPEAHVQL PPQAQASDYA KILAHYHDVG GLKPALVVTS
GNDDARLVLD DGRNVQLKLD AVAWAQKYLK PRYRGPKPKH VDDVLKPGDI VRLRKDDKGQ
WQLAQIPAAQ SGLVSLNPDD GAVLALVGGF SFQRSKFNRA LMTGSGRQPG SSFKPFIYSA
AFEHGFTPAT IINDAPVVLP DPSKPNGQWT PSNDDGKFDG PIRLRTALIK SKNLVSVRLL
DTLGLQFARQ YALRFGFDPD AVPDNLSMAL GTASVSPMTM ARAYAVFANG GFLVEPYFIQ
EIDNRDGQTI YKANPLRACR DCQARLLQSS DASDTLPPAP SSSVAAAASY AGTDGLLPLQ
PIASSSSPQP AEASSTAEPR LAPRVINIRN DYLTTSLMKD VILHGTGIAA RALNRPDLAG
KTGTTNEHRD AWFCGFNDKV VTTVWVGFDN FSTLGYEFGA TAALPIWMDY MGAALKGTPE
SALPRPPGIT SLLINRNTGL PTTADDPDAM PEIFKVEDVP HLQELARKAK QDQNQKHAYD
IF
//
