ID G1C782_ACIBA Unreviewed; 851 AA.
AC G1C782;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 24-JAN-2024, entry version 56.
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:AEK25754.1};
GN ORFNames=APD31_05775 {ECO:0000313|EMBL:KQD99841.1};
OS Acinetobacter baumannii.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Acinetobacter; Acinetobacter calcoaceticus/baumannii complex.
OX NCBI_TaxID=470 {ECO:0000313|EMBL:AEK25754.1};
RN [1] {ECO:0000313|EMBL:AEK25754.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=HUMV-2120 {ECO:0000313|EMBL:AEK25756.1}, HUMV-2471
RC {ECO:0000313|EMBL:AEK25753.1}, HUMV-4066
RC {ECO:0000313|EMBL:AEK25754.1}, HUMV-6457
RC {ECO:0000313|EMBL:AEK25755.1}, and HUS-457
RC {ECO:0000313|EMBL:AEK25771.1};
RA Cayo R., Rodriguez M.-C., Espinal P., Fernandez-Cuenca F., Ocampo-Sosa A.,
RA Pascual A., Ayala J.A., Vila J., Martinez-Martinez L.;
RT "Analysis of Genes Encoding for Penicillin-Binding Proteins in Clinical
RT Isolates of Acinetobacter baumannii.";
RL Submitted (MAR-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQD99841.1, ECO:0000313|Proteomes:UP000050896}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ABBL070 {ECO:0000313|EMBL:KQD99841.1,
RC ECO:0000313|Proteomes:UP000050896};
RA Ozer E.A., Fitzpatrick M.A., Hauser A.R.;
RT "The utility of whole genome sequencing in characterizing Acinetobacter
RT epidemiology and analyzing hospital outbreaks.";
RL Submitted (OCT-2015) 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 ---------------------------------------------------------------------------
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; JF746084; AEK25753.1; -; Genomic_DNA.
DR EMBL; JF746085; AEK25754.1; -; Genomic_DNA.
DR EMBL; JF746086; AEK25755.1; -; Genomic_DNA.
DR EMBL; JF746087; AEK25756.1; -; Genomic_DNA.
DR EMBL; JF746102; AEK25771.1; -; Genomic_DNA.
DR EMBL; LLGA01000023; KQD99841.1; -; Genomic_DNA.
DR RefSeq; WP_000736674.1; NZ_WJSY01000002.1.
DR AlphaFoldDB; G1C782; -.
DR SMR; G1C782; -.
DR PATRIC; fig|470.1737.peg.315; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000050896; 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 Membrane {ECO:0000256|SAM:Phobius};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
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 321..419
FT /note="Penicillin-binding protein OB-like"
FT /evidence="ECO:0000259|Pfam:PF17092"
FT DOMAIN 424..737
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
FT REGION 791..851
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 834..851
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 851 AA; 94738 MW; 29542499F8F6D063 CRC64;
MKKLSSLGFV RPIFLIIIII LVSLPMGFYG MYLYIAPTLP EMSSLKKAPL LKPLQVYTAD
NQLIAEYGGK LSIPVEYKQI PPNFIHAFLA AEDSSFFEHS GISFKGLGRA LSESVTGSDV
QTGGSTITMQ VAKNYYLSPE RTLKRKLTEI FLARKIEQNL SKEDILSLYV NKIFLGKNAY
GIAAAAKIYY NKSINELSIA QMAMIAGLPK APSKYNPVVN PERALERRNW ILGRMLQLGY
ISQAEYQKAV AEPINLNMPN RDLNNIHPYA GEMVRSELVK HFGEQAIDSG YKVYTTINAK
RQAIAEKAVQ DGLEAYDRRH GWRGAEAHDK PLSEFRAYAN TYPAQVTKVN SSSFEALMQD
GSTVTVQWSG MSWARPYRNA NSVGAAPSRA SQIVKVKDIV RLRPNEAKTA WSLVQVPKVQ
GQLIAINPND GSIEAIVGGY NFYQSKFNRA LQGWRQPGST IKPFLYALAL ERGMTPYSMV
NDSPITIGKW TPKNSDGRYL GMIPLRRALY LSRNTVSVRL LQTVGIERTR QLFMDFGLQE
DQIPRNYTIA LGTPQVLPIQ MATGYATFAN GGYRVQPHFI QRIEDAYGKV IYEAKPEYAC
IPCINAPETT DDAQVTTPDD QVVEVTNKEL EQKEKATKQL NLKQTDKNNS QYRQAQRILK
SSSAYDMANI LRDVIEHGTG RAALKIGRSD LGGKTGTTND AKDAWFAGFN GKLVTVTWVG
FDQPTTLGRR EYGGIAALPI WINFMGQALQ GTPAAWVRLE KDAQAPISRD KQEVTTEVGD
KKTYRAAPPL ARPLYRPAPP QPKTTNNDFD DLPGEEIVIP SKTTPPAMKP SQGAAPKREK
DELENLINQI E
//