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Penicillin-binding protein 1A (PBP-1a) (PBP1a) [Includes: Penicillin-insensitive transglycosylase (EC 2.4.1.129) (Peptidoglycan TGase); Penicillin-sensitive transpeptidase (EC 3.4.16.4) (DD-transpeptidase)]

 PBPA_AQUAE              Reviewed;         726 AA.
O66874;
20-JUN-2001, integrated into UniProtKB/Swiss-Prot.
01-AUG-1998, sequence version 1.
28-FEB-2018, entry version 128.
RecName: Full=Penicillin-binding protein 1A;
Short=PBP-1a;
Short=PBP1a;
Includes:
RecName: Full=Penicillin-insensitive transglycosylase;
EC=2.4.1.129 {ECO:0000250|UniProtKB:P02918};
AltName: Full=Peptidoglycan TGase;
Includes:
RecName: Full=Penicillin-sensitive transpeptidase;
EC=3.4.16.4 {ECO:0000250|UniProtKB:P02918};
AltName: Full=DD-transpeptidase;
Name=mrcA; Synonyms=ponA; OrderedLocusNames=aq_624;
Aquifex aeolicus (strain VF5).
Bacteria; Aquificae; Aquificales; Aquificaceae; Aquifex.
NCBI_TaxID=224324;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=VF5;
PubMed=9537320; DOI=10.1038/32831;
Deckert G., Warren P.V., Gaasterland T., Young W.G., Lenox A.L.,
Graham D.E., Overbeek R., Snead M.A., Keller M., Aujay M., Huber R.,
Feldman R.A., Short J.M., Olsen G.J., Swanson R.V.;
"The complete genome of the hyperthermophilic bacterium Aquifex
aeolicus.";
Nature 392:353-358(1998).
-!- CATALYTIC ACTIVITY: (GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-
Lys-D-Ala-D-Ala))(n)-diphosphoundecaprenol + GlcNAc-(1->4)-
Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-
diphosphoundecaprenol = (GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-
Glu-L-Lys-D-Ala-D-Ala))(n+1)-diphosphoundecaprenol + undecaprenyl
diphosphate. {ECO:0000250|UniProtKB:P02918}.
-!- CATALYTIC ACTIVITY: Preferential cleavage: (Ac)(2)-L-Lys-D-Ala-|-
D-Ala. Also transpeptidation of peptidyl-alanyl moieties that are
N-acyl substituents of D-alanine. {ECO:0000250|UniProtKB:P02918}.
-!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
-!- INTERACTION:
Self; NbExp=2; IntAct=EBI-15625175, EBI-15625175;
-!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000250}; Single-
pass type II membrane protein {ECO:0000250}.
-!- SIMILARITY: In the N-terminal section; belongs to the
glycosyltransferase 51 family. {ECO:0000305}.
-!- SIMILARITY: In the C-terminal section; belongs to the
transpeptidase family. {ECO:0000305}.
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EMBL; AE000657; AAC06835.1; -; Genomic_DNA.
PIR; F70355; F70355.
RefSeq; NP_213434.1; NC_000918.1.
RefSeq; WP_010880372.1; NC_000918.1.
PDB; 2OQO; X-ray; 2.10 A; A=51-243.
PDB; 3D3H; X-ray; 2.31 A; A=51-243.
PDB; 3NB6; X-ray; 2.70 A; A=51-243.
PDB; 3NB7; X-ray; 2.65 A; A=51-243.
PDBsum; 2OQO; -.
PDBsum; 3D3H; -.
PDBsum; 3NB6; -.
PDBsum; 3NB7; -.
ProteinModelPortal; O66874; -.
SMR; O66874; -.
DIP; DIP-60897N; -.
STRING; 224324.aq_624; -.
CAZy; GT51; Glycosyltransferase Family 51.
EnsemblBacteria; AAC06835; AAC06835; aq_624.
GeneID; 1193936; -.
KEGG; aae:aq_624; -.
PATRIC; fig|224324.8.peg.507; -.
eggNOG; ENOG4108JQC; Bacteria.
eggNOG; COG5009; LUCA.
HOGENOM; HOG000041137; -.
InParanoid; O66874; -.
KO; K05366; -.
OMA; LAQMAMI; -.
OrthoDB; POG091H01NC; -.
BioCyc; AAEO224324:G1G15-452-MONOMER; -.
BRENDA; 2.4.1.129; 396.
UniPathway; UPA00219; -.
EvolutionaryTrace; O66874; -.
Proteomes; UP000000798; Chromosome.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0008658; F:penicillin binding; IEA:InterPro.
GO; GO:0008955; F:peptidoglycan glycosyltransferase activity; IEA:UniProtKB-EC.
GO; GO:0009002; F:serine-type D-Ala-D-Ala carboxypeptidase activity; IEA:UniProtKB-EC.
GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-UniPathway.
GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
GO; GO:0046677; P:response to antibiotic; IEA:UniProtKB-KW.
Gene3D; 1.10.3810.10; -; 1.
InterPro; IPR012338; Beta-lactam/transpept-like.
InterPro; IPR001264; Glyco_trans_51.
InterPro; IPR023346; Lysozyme-like_dom_sf.
InterPro; IPR036950; PBP_transglycosylase.
InterPro; IPR001460; PCN-bd_Tpept.
Pfam; PF00912; Transgly; 1.
Pfam; PF00905; Transpeptidase; 1.
SUPFAM; SSF53955; SSF53955; 1.
SUPFAM; SSF56601; SSF56601; 3.
1: Evidence at protein level;
3D-structure; Antibiotic resistance; Carboxypeptidase;
Cell inner membrane; Cell membrane; Cell shape;
Cell wall biogenesis/degradation; Complete proteome;
Glycosyltransferase; Hydrolase; Membrane; Multifunctional enzyme;
Peptidoglycan synthesis; Protease; Reference proteome; Signal-anchor;
Transferase; Transmembrane; Transmembrane helix.
CHAIN 1 726 Penicillin-binding protein 1A.
/FTId=PRO_0000083178.
TOPO_DOM 1 3 Cytoplasmic. {ECO:0000255}.
TRANSMEM 4 24 Helical; Signal-anchor for type II
membrane protein. {ECO:0000255}.
TOPO_DOM 25 726 Periplasmic. {ECO:0000255}.
REGION 45 213 Transglycosylase.
REGION 379 662 Transpeptidase.
ACT_SITE 83 83 Proton donor; for transglycosylase
activity. {ECO:0000250|UniProtKB:P02919}.
ACT_SITE 432 432 Acyl-ester intermediate; for
transpeptidase activity.
{ECO:0000250|UniProtKB:P02919}.
HELIX 60 62 {ECO:0000244|PDB:2OQO}.
HELIX 68 70 {ECO:0000244|PDB:2OQO}.
HELIX 73 83 {ECO:0000244|PDB:2OQO}.
TURN 85 89 {ECO:0000244|PDB:2OQO}.
STRAND 90 93 {ECO:0000244|PDB:2OQO}.
HELIX 95 102 {ECO:0000244|PDB:2OQO}.
HELIX 118 124 {ECO:0000244|PDB:2OQO}.
STRAND 127 129 {ECO:0000244|PDB:2OQO}.
HELIX 134 150 {ECO:0000244|PDB:2OQO}.
HELIX 153 163 {ECO:0000244|PDB:2OQO}.
HELIX 173 181 {ECO:0000244|PDB:2OQO}.
HELIX 185 187 {ECO:0000244|PDB:2OQO}.
HELIX 190 198 {ECO:0000244|PDB:2OQO}.
HELIX 203 206 {ECO:0000244|PDB:2OQO}.
TURN 208 210 {ECO:0000244|PDB:2OQO}.
HELIX 212 228 {ECO:0000244|PDB:2OQO}.
HELIX 234 241 {ECO:0000244|PDB:2OQO}.
SEQUENCE 726 AA; 81824 MW; 37F756397C9D7B38 CRC64;
MKKLVIGILG IVIALFVGLL VFLIPIYKNL PDPKLLESWT PPQASEVYDA KGRLYGTIGI
QKRFYVSIDK IPEHVINAFV ATEDRNFWHH FGIDPVAIVR AAIVNYRAGR IVQGGSTITQ
QLAKNLFLTR ERTLERKIKE ALLAIKIERT FDKKKIMELY LNQIYLGSGA YGVEAAAQVY
FGKHVWELSL DEAALLAALP KAPAKYNPFY HPERALQRRN LVLKRMLEEG YITPEQYEEA
VNKPLTVKKE NKYKFSDYFL DMVKSYVFNK YGEIAYKGRL KIYTTIDLDY QKIAQKSLEE
GLKRVAKIIG LPFLPKSEED MELAYEKEAQ LKRLKRGKIY VAKILKYDGN FMKVEIHGKK
LKGEIKGLNT EGHKYVFVKY LGGNRAEIIP DLEGSLVSID VKTGEIKAIV GGRSYAYSQF
NRAVKALRQP GSAIKPVIYL SALLKGMTQI STIDASSKPY YDPSKGEDWI PKNYDEKEYG
NVTLRYALAH SINTAAVNLL DKVGFELVLE VGKKVGLDNL KPYYSLALGT VEVTPLQLTA
AYQVFANLGT ECKPFFIKKI VDENGEVLEE NVPECEEVLP KPETRVPVDM LRAVVLEGTA
RRASVLDRIV AGKTGTTDDF QDAWFVGFSP YIVTGVWVGY DVKKSLGKHM SGSRVALPIW
IDYMKVVTRM YPNEDFELPP ENIVVNINPK DLVLADETCE GVPMVFVKGT EPHITCSDLN
AILGLR


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