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 02-SEP-2026, entry version 114. DE RecName: Full=Penicillin-binding protein 1A {ECO:0000256|ARBA:ARBA00018638}; DE EC=2.4.99.28 {ECO:0000256|ARBA:ARBA00044770}; DE EC=3.4.16.4 {ECO:0000256|ARBA:ARBA00012448}; GN OrderedLocusNames=ACIAD3361 {ECO:0000313|EMBL:CAG70027.1}; OS Acinetobacter baylyi (strain ATCC 33305 / BD413 / ADP1). OC Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria; OC Moraxellales; Moraxellaceae; Acinetobacter. OX NCBI_TaxID=62977 {ECO:0000313|EMBL:CAG70027.1, ECO:0000313|Proteomes:UP000000430}; RN [1] {ECO:0000313|EMBL:CAG70027.1, ECO:0000313|Proteomes:UP000000430} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33305 / BD413 / 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). 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=2.4.99.28; CC Evidence={ECO:0000256|ARBA:ARBA00049902}; CC -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis. CC {ECO:0000256|ARBA:ARBA00004752}. CC -!- PATHWAY: Glycan biosynthesis. {ECO:0000256|ARBA:ARBA00060592}. CC -!- SUBCELLULAR LOCATION: Cell inner membrane CC {ECO:0000256|ARBA:ARBA00004249}; Single-pass type II membrane protein CC {ECO:0000256|ARBA:ARBA00004249}. 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 --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 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:0030288; C:outer membrane-bounded periplasmic space; IEA:TreeGrafter. 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 FunFam; 1.10.3810.10:FF:000003; Penicillin-binding protein 1a; 1. 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; IPR050396; Glycosyltr_51/Transpeptidase. DR InterPro; IPR023346; Lysozyme-like_dom_sf. DR InterPro; IPR031376; PCB_OB. DR InterPro; IPR001460; PCN-bd_Tpept. DR InterPro; IPR036950; Transglycosylase. 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 Cell inner membrane {ECO:0000256|ARBA:ARBA00022519}; KW Cell membrane {ECO:0000256|ARBA:ARBA00022475}; KW Cell shape {ECO:0000256|ARBA:ARBA00022960}; KW Cell wall biogenesis/degradation {ECO:0000256|ARBA:ARBA00023316}; KW Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676}; KW Hydrolase {ECO:0000256|ARBA:ARBA00022801}; KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius}; KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268}; KW Peptidoglycan synthesis {ECO:0000256|ARBA:ARBA00022984}; KW Protease {ECO:0000256|ARBA:ARBA00022670}; KW Reference proteome {ECO:0000313|Proteomes:UP000000430}; KW Signal-anchor {ECO:0000256|ARBA:ARBA00022968}; KW Transferase {ECO:0000256|ARBA:ARBA00022679}; KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, KW 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 322..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 766..780 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 817..832 FT /note="Low complexity" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 833..843 FT /note="Basic and acidic 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 //