PBPA_AQUAE
ID PBPA_AQUAE Reviewed; 726 AA.
AC O66874;
DT 20-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=Penicillin-binding protein 1A;
DE Short=PBP-1a;
DE Short=PBP1a;
DE Includes:
DE RecName: Full=Penicillin-insensitive transglycosylase;
DE EC=2.4.1.129 {ECO:0000250|UniProtKB:P02918};
DE AltName: Full=Peptidoglycan TGase;
DE Includes:
DE RecName: Full=Penicillin-sensitive transpeptidase;
DE EC=3.4.16.4 {ECO:0000250|UniProtKB:P02918};
DE AltName: Full=DD-transpeptidase;
GN Name=mrcA; Synonyms=ponA; OrderedLocusNames=aq_624;
OS Aquifex aeolicus (strain VF5).
OC Bacteria; Aquificae; Aquificales; Aquificaceae; Aquifex.
OX NCBI_TaxID=224324;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VF5;
RX PubMed=9537320; DOI=10.1038/32831;
RA Deckert G., Warren P.V., Gaasterland T., Young W.G., Lenox A.L.,
RA Graham D.E., Overbeek R., Snead M.A., Keller M., Aujay M., Huber R.,
RA Feldman R.A., Short J.M., Olsen G.J., Swanson R.V.;
RT "The complete genome of the hyperthermophilic bacterium Aquifex aeolicus.";
RL Nature 392:353-358(1998).
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:0000250|UniProtKB:P02918};
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:0000250|UniProtKB:P02918};
CC -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC -!- INTERACTION:
CC O66874; O66874: mrcA; NbExp=2; IntAct=EBI-15625175, EBI-15625175;
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000250}; Single-pass
CC type II membrane protein {ECO:0000250}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the
CC glycosyltransferase 51 family. {ECO:0000305}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the transpeptidase
CC family. {ECO:0000305}.
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DR EMBL; AE000657; AAC06835.1; -; Genomic_DNA.
DR PIR; F70355; F70355.
DR RefSeq; NP_213434.1; NC_000918.1.
DR RefSeq; WP_010880372.1; NC_000918.1.
DR PDB; 2OQO; X-ray; 2.10 A; A=51-243.
DR PDB; 3D3H; X-ray; 2.31 A; A=51-243.
DR PDB; 3NB6; X-ray; 2.70 A; A=51-243.
DR PDB; 3NB7; X-ray; 2.65 A; A=51-243.
DR PDBsum; 2OQO; -.
DR PDBsum; 3D3H; -.
DR PDBsum; 3NB6; -.
DR PDBsum; 3NB7; -.
DR AlphaFoldDB; O66874; -.
DR SMR; O66874; -.
DR DIP; DIP-60897N; -.
DR STRING; 224324.aq_624; -.
DR CAZy; GT51; Glycosyltransferase Family 51.
DR EnsemblBacteria; AAC06835; AAC06835; aq_624.
DR KEGG; aae:aq_624; -.
DR PATRIC; fig|224324.8.peg.507; -.
DR eggNOG; COG5009; Bacteria.
DR HOGENOM; CLU_006354_2_4_0; -.
DR InParanoid; O66874; -.
DR OMA; LAQMAMI; -.
DR OrthoDB; 652304at2; -.
DR BRENDA; 2.4.1.129; 396.
DR UniPathway; UPA00219; -.
DR EvolutionaryTrace; O66874; -.
DR Proteomes; UP000000798; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0008658; F:penicillin binding; IBA:GO_Central.
DR GO; GO:0008955; F:peptidoglycan glycosyltransferase activity; IBA:GO_Central.
DR GO; GO:0009002; F:serine-type D-Ala-D-Ala carboxypeptidase activity; IEA:UniProtKB-EC.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0009252; P:peptidoglycan biosynthetic process; IBA:GO_Central.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
DR GO; GO:0046677; P:response to antibiotic; IBA:GO_Central.
DR Gene3D; 1.10.3810.10; -; 1.
DR Gene3D; 3.40.710.10; -; 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; IPR001460; PCN-bd_Tpept.
DR Pfam; PF00912; Transgly; 1.
DR Pfam; PF00905; Transpeptidase; 1.
DR SUPFAM; SSF53955; SSF53955; 1.
DR SUPFAM; SSF56601; SSF56601; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Antibiotic resistance; Carboxypeptidase; Cell inner membrane;
KW Cell membrane; Cell shape; Cell wall biogenesis/degradation;
KW Glycosyltransferase; Hydrolase; Membrane; Multifunctional enzyme;
KW Peptidoglycan synthesis; Protease; Reference proteome; Signal-anchor;
KW Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..726
FT /note="Penicillin-binding protein 1A"
FT /id="PRO_0000083178"
FT TOPO_DOM 1..3
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 4..24
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 25..726
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT REGION 45..213
FT /note="Transglycosylase"
FT REGION 379..662
FT /note="Transpeptidase"
FT ACT_SITE 83
FT /note="Proton donor; for transglycosylase activity"
FT /evidence="ECO:0000250|UniProtKB:P02919"
FT ACT_SITE 432
FT /note="Acyl-ester intermediate; for transpeptidase
FT activity"
FT /evidence="ECO:0000250|UniProtKB:P02919"
FT HELIX 60..62
FT /evidence="ECO:0007829|PDB:2OQO"
FT HELIX 68..70
FT /evidence="ECO:0007829|PDB:2OQO"
FT HELIX 73..83
FT /evidence="ECO:0007829|PDB:2OQO"
FT TURN 85..89
FT /evidence="ECO:0007829|PDB:2OQO"
FT STRAND 90..93
FT /evidence="ECO:0007829|PDB:2OQO"
FT HELIX 95..102
FT /evidence="ECO:0007829|PDB:2OQO"
FT HELIX 118..124
FT /evidence="ECO:0007829|PDB:2OQO"
FT STRAND 127..129
FT /evidence="ECO:0007829|PDB:2OQO"
FT HELIX 134..150
FT /evidence="ECO:0007829|PDB:2OQO"
FT HELIX 153..163
FT /evidence="ECO:0007829|PDB:2OQO"
FT HELIX 173..181
FT /evidence="ECO:0007829|PDB:2OQO"
FT HELIX 185..187
FT /evidence="ECO:0007829|PDB:2OQO"
FT HELIX 190..198
FT /evidence="ECO:0007829|PDB:2OQO"
FT HELIX 203..206
FT /evidence="ECO:0007829|PDB:2OQO"
FT TURN 208..210
FT /evidence="ECO:0007829|PDB:2OQO"
FT HELIX 212..228
FT /evidence="ECO:0007829|PDB:2OQO"
FT HELIX 234..241
FT /evidence="ECO:0007829|PDB:2OQO"
SQ 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
