ID Q9AM64_ACIAD Unreviewed; 852 AA.
AC Q9AM64; Q6F7D8;
DT 01-JUN-2001, integrated into UniProtKB/TrEMBL.
DT 01-JUN-2001, sequence version 1.
DT 27-MAR-2024, entry version 103.
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 Name=ponA {ECO:0000313|EMBL:AAK00346.1};
GN OrderedLocusNames=ACIAD3361 {ECO:0000313|EMBL:CAG70027.1};
OS Acinetobacter baylyi (strain ATCC 33305 / BD413 / ADP1).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Acinetobacter.
OX NCBI_TaxID=62977 {ECO:0000313|EMBL:AAK00346.1};
RN [1] {ECO:0000313|EMBL:AAK00346.1}
RP NUCLEOTIDE SEQUENCE.
RA Rosenplaenter C., Averhoff B.;
RT "Genes essential for the natural transformation process in Acinetobacter
RT sp. BD413.";
RL Submitted (DEC-2000) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:CAG70027.1, ECO:0000313|Proteomes:UP000000430}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ADP1 {ECO:0000313|EMBL:CAG70027.1}, and ATCC 33305 / BD413 /
RC ADP1 {ECO:0000313|Proteomes:UP000000430};
RX PubMed=15514110; DOI=10.1093/nar/gkh910;
RA Barbe V., Vallenet D., Fonknechten N., Kreimeyer A., Oztas S., Labarre L.,
RA Cruveiller S., Robert C., Duprat S., Wincker P., Ornston L.N.,
RA Weissenbach J., Marliere P., Cohen G.N., Medigue C.;
RT "Unique features revealed by the genome sequence of Acinetobacter sp. ADP1,
RT a versatile and naturally transformation competent bacterium.";
RL Nucleic Acids Res. 32:5766-5779(2004).
RN [3] {ECO:0000313|EMBL:CAG70027.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=ADP1 {ECO:0000313|EMBL:CAG70027.1};
RA Genoscope;
RL Submitted (JUN-2004) 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; AF329876; AAK00346.1; -; Genomic_DNA.
DR EMBL; CR543861; CAG70027.1; -; Genomic_DNA.
DR RefSeq; WP_004923711.1; NC_005966.1.
DR AlphaFoldDB; Q9AM64; -.
DR STRING; 202950.GCA_001485005_02199; -.
DR CAZy; GT51; Glycosyltransferase Family 51.
DR DNASU; 2878085; -.
DR GeneID; 45235555; -.
DR KEGG; aci:ACIAD3361; -.
DR eggNOG; COG5009; Bacteria.
DR HOGENOM; CLU_006354_2_4_6; -.
DR OrthoDB; 9766909at2; -.
DR BioCyc; ASP62977:ACIAD_RS15200-MONOMER; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000000430; 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; 3.
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 Membrane {ECO:0000256|SAM:Phobius};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000000430};
KW Signal-anchor {ECO:0000256|ARBA:ARBA00022968};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..35
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 62..235
FT /note="Glycosyl transferase family 51"
FT /evidence="ECO:0000259|Pfam:PF00912"
FT DOMAIN 325..419
FT /note="Penicillin-binding protein OB-like"
FT /evidence="ECO:0000259|Pfam:PF17092"
FT DOMAIN 424..743
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
FT REGION 766..852
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 819..834
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 852 AA; 94815 MW; F7FF6668DF6E6D96 CRC64;
MKKLSSSGRV HPFFLLILMV LVSVPMGFYG MYLYIAPSLP EMSSLKKAPL LKPLQVYTSD
NQLIAEYGGK LSVPVEYNQI PPTFIHAFLA AEDSSFFEHS GISFKGLGRA LSETVTGSNV
QTGGSTITMQ VAKNYYLSPE RTLKRKLTEI FLARKIEQNL TKQEILSLYV NKIFLGKNAY
GIAAAAKIYY NKTLDQLSIA EMAMISGLPK APSKYNPVVN PERALERRNW ILGRMLQLGY
INQTQYQQAV AEPINLDMPD RGVSNRYPYI GEMVRAELVE KFGEQAVDSG YKVYTTINSQ
RQAYAEQSVQ DGLEAYDRRH GWRGAEAHDK PLRNFIPYAN TFPAEVIKVG NNSFDALMQD
GKTVTVPWSG MSWARRYRNA NSVGESPSRA SQIVKVKDIV RLRPNGDKSA WSLVQIPKVQ
GQLIALNPND GSIEALVGGY NFYQSKFNRA LQGWRQPGST IKPFIYALAL ERGMTPYTMV
NDSPISIGRW SPKNSDGRYL GMIPLRRALY LSRNTVSVRL LQSVGVERAR QLLMDFGLQE
NQIPRNFTIA LGTPQVLPIQ MATGYATFAN GGYRIQPHFI RRIEDAYGNV IFETKPEYAC
IPCINETNNT ETEIKPQTPD DEVIEVNNQS LDEAKTLVSP AKTNPDNNNY RQAQRILKSS
SAYDMANILR DVILHGTGRA ALKIGRDDLG GKTGTTNDAK DAWFAGFNGK LVAVAWVGFD
QPTTLGRREY GGVAALPIWT NFMDQSLKGT PSAWVRFDKN AKAPLSREKP TIEIQNREDD
QASPPLARPL YVPAPVTPAR TPDSDFADLP GEEILVPSQG QPPSMQQQPS SPKKNETPKR
GDALEGLINQ VT
//
