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Database: UniProt
Entry: G1C782_ACIBA
LinkDB: G1C782_ACIBA
Original site: G1C782_ACIBA 
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}.
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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
//
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