PBPA_STRPN
ID PBPA_STRPN Reviewed; 719 AA.
AC Q04707;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 26-SEP-2001, sequence version 2.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=Penicillin-binding protein 1A;
DE Short=PBP-1A;
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=ponA; OrderedLocusNames=SP_0369;
OS Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=170187;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=45607, and 63915;
RX PubMed=1396576; DOI=10.1002/j.1460-2075.1992.tb05475.x;
RA Martin C., Sibold C., Hakenbeck R.;
RT "Relatedness of penicillin-binding protein 1a genes from different clones
RT of penicillin-resistant Streptococcus pneumoniae isolated in South Africa
RT and Spain.";
RL EMBO J. 11:3831-3836(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-334 / TIGR4;
RX PubMed=11463916; DOI=10.1126/science.1061217;
RA Tettelin H., Nelson K.E., Paulsen I.T., Eisen J.A., Read T.D.,
RA Peterson S.N., Heidelberg J.F., DeBoy R.T., Haft D.H., Dodson R.J.,
RA Durkin A.S., Gwinn M.L., Kolonay J.F., Nelson W.C., Peterson J.D.,
RA Umayam L.A., White O., Salzberg S.L., Lewis M.R., Radune D.,
RA Holtzapple E.K., Khouri H.M., Wolf A.M., Utterback T.R., Hansen C.L.,
RA McDonald L.A., Feldblyum T.V., Angiuoli S.V., Dickinson T., Hickey E.K.,
RA Holt I.E., Loftus B.J., Yang F., Smith H.O., Venter J.C., Dougherty B.A.,
RA Morrison D.A., Hollingshead S.K., Fraser C.M.;
RT "Complete genome sequence of a virulent isolate of Streptococcus
RT pneumoniae.";
RL Science 293:498-506(2001).
CC -!- FUNCTION: Cell wall formation.
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 -!- SUBCELLULAR LOCATION: Secreted.
CC -!- MISCELLANEOUS: These strains are penicillin-sensitive.
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; X67873; CAA48073.1; -; Genomic_DNA.
DR EMBL; X67872; CAA48072.1; -; Genomic_DNA.
DR EMBL; AE005672; AAK74536.1; -; Genomic_DNA.
DR PIR; G95042; G95042.
DR PIR; S28037; S28037.
DR PIR; S28038; S28038.
DR RefSeq; WP_001040013.1; NZ_AKVY01000001.1.
DR PDB; 2ZC5; X-ray; 3.00 A; A/C=47-70, B/D=264-653.
DR PDB; 2ZC6; X-ray; 2.70 A; A/C=47-70, B/D=264-653.
DR PDBsum; 2ZC5; -.
DR PDBsum; 2ZC6; -.
DR AlphaFoldDB; Q04707; -.
DR SMR; Q04707; -.
DR STRING; 170187.SP_0369; -.
DR BindingDB; Q04707; -.
DR ChEMBL; CHEMBL1255141; -.
DR DrugBank; DB01150; Cefprozil.
DR DrugBank; DB05659; Faropenem medoxomil.
DR CAZy; GT51; Glycosyltransferase Family 51.
DR EnsemblBacteria; AAK74536; AAK74536; SP_0369.
DR KEGG; spn:SP_0369; -.
DR eggNOG; COG0744; Bacteria.
DR OMA; LAQMAMI; -.
DR PhylomeDB; Q04707; -.
DR BioCyc; SPNE170187:G1FZB-380-MON; -.
DR UniPathway; UPA00219; -.
DR EvolutionaryTrace; Q04707; -.
DR PRO; PR:Q04707; -.
DR Proteomes; UP000000585; Chromosome.
DR GO; GO:0005576; C:extracellular region; 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:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-UniPathway.
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; IEA:UniProtKB-KW.
DR Gene3D; 1.10.3810.10; -; 1.
DR Gene3D; 3.40.710.10; -; 1.
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 shape;
KW Cell wall biogenesis/degradation; Glycosyltransferase; Hydrolase;
KW Multifunctional enzyme; Peptidoglycan synthesis; Protease; Secreted;
KW Transferase.
FT CHAIN 1..719
FT /note="Penicillin-binding protein 1A"
FT /id="PRO_0000083182"
FT REGION 62..223
FT /note="Transglycosylase"
FT /evidence="ECO:0000250|UniProtKB:P02919"
FT REGION 297..611
FT /note="Transpeptidase"
FT /evidence="ECO:0000250|UniProtKB:P02919"
FT REGION 652..719
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 91
FT /note="Proton donor; for transglycosylase activity"
FT /evidence="ECO:0000250|UniProtKB:P02919"
FT ACT_SITE 370
FT /note="Acyl-ester intermediate; for transpeptidase
FT activity"
FT /evidence="ECO:0000250|UniProtKB:P02919"
FT VARIANT 386
FT /note="V -> I (in strain: 63915)"
FT VARIANT 397
FT /note="E -> K (in strain: 63915)"
FT VARIANT 523
FT /note="M -> I (in strain: 63915)"
FT VARIANT 533
FT /note="D -> E (in strain: 45607)"
FT VARIANT 540
FT /note="T -> S (in strain: 63915)"
FT VARIANT 657
FT /note="N -> S (in strain: 45607)"
FT STRAND 54..56
FT /evidence="ECO:0007829|PDB:2ZC6"
FT STRAND 62..65
FT /evidence="ECO:0007829|PDB:2ZC6"
FT HELIX 270..272
FT /evidence="ECO:0007829|PDB:2ZC6"
FT HELIX 273..287
FT /evidence="ECO:0007829|PDB:2ZC6"
FT TURN 291..293
FT /evidence="ECO:0007829|PDB:2ZC6"
FT STRAND 296..300
FT /evidence="ECO:0007829|PDB:2ZC6"
FT HELIX 304..315
FT /evidence="ECO:0007829|PDB:2ZC6"
FT STRAND 316..319
FT /evidence="ECO:0007829|PDB:2ZC6"
FT STRAND 328..335
FT /evidence="ECO:0007829|PDB:2ZC6"
FT TURN 336..338
FT /evidence="ECO:0007829|PDB:2ZC6"
FT STRAND 340..345
FT /evidence="ECO:0007829|PDB:2ZC6"
FT TURN 360..362
FT /evidence="ECO:0007829|PDB:2ZC6"
FT HELIX 369..371
FT /evidence="ECO:0007829|PDB:2ZC6"
FT HELIX 372..376
FT /evidence="ECO:0007829|PDB:2ZC6"
FT HELIX 378..383
FT /evidence="ECO:0007829|PDB:2ZC6"
FT STRAND 393..398
FT /evidence="ECO:0007829|PDB:2ZC6"
FT STRAND 417..420
FT /evidence="ECO:0007829|PDB:2ZC6"
FT HELIX 421..427
FT /evidence="ECO:0007829|PDB:2ZC6"
FT HELIX 431..440
FT /evidence="ECO:0007829|PDB:2ZC6"
FT HELIX 442..450
FT /evidence="ECO:0007829|PDB:2ZC6"
FT TURN 451..453
FT /evidence="ECO:0007829|PDB:2ZC6"
FT HELIX 461..464
FT /evidence="ECO:0007829|PDB:2ZC6"
FT STRAND 473..477
FT /evidence="ECO:0007829|PDB:2ZC6"
FT HELIX 480..491
FT /evidence="ECO:0007829|PDB:2ZC6"
FT STRAND 494..496
FT /evidence="ECO:0007829|PDB:2ZC6"
FT STRAND 502..507
FT /evidence="ECO:0007829|PDB:2ZC6"
FT STRAND 512..514
FT /evidence="ECO:0007829|PDB:2ZC6"
FT STRAND 519..521
FT /evidence="ECO:0007829|PDB:2ZC5"
FT HELIX 525..540
FT /evidence="ECO:0007829|PDB:2ZC6"
FT TURN 543..546
FT /evidence="ECO:0007829|PDB:2ZC6"
FT STRAND 555..560
FT /evidence="ECO:0007829|PDB:2ZC6"
FT HELIX 565..570
FT /evidence="ECO:0007829|PDB:2ZC6"
FT STRAND 578..587
FT /evidence="ECO:0007829|PDB:2ZC6"
FT STRAND 589..598
FT /evidence="ECO:0007829|PDB:2ZC6"
FT HELIX 608..612
FT /evidence="ECO:0007829|PDB:2ZC6"
FT HELIX 613..626
FT /evidence="ECO:0007829|PDB:2ZC6"
FT STRAND 640..643
FT /evidence="ECO:0007829|PDB:2ZC6"
FT STRAND 646..649
FT /evidence="ECO:0007829|PDB:2ZC6"
SQ SEQUENCE 719 AA; 79759 MW; 5BD397E83B4B3AA6 CRC64;
MNKPTILRLI KYLSISFLSL VIAAIVLGGG VFFYYVSKAP SLSESKLVAT TSSKIYDNKN
QLIADLGSER RVNAQANDIP TDLVKAIVSI EDHRFFDHRG IDTIRILGAF LRNLQSNSLQ
GGSTLTQQLI KLTYFSTSTS DQTISRKAQE AWLAIQLEQK ATKQEILTYY INKVYMSNGN
YGMQTAAQNY YGKDLNNLSL PQLALLAGMP QAPNQYDPYS HPEAAQDRRN LVLSEMKNQG
YISAEQYEKA VNTPITDGLQ SLKSASNYPA YMDNYLKEVI NQVEEETGYN LLTTGMDVYT
NVDQEAQKHL WDIYNTDEYV AYPDDELQVA STIVDVSNGK VIAQLGARHQ SSNVSFGINQ
AVETNRDWGS TMKPITDYAP ALEYGVYDST ATIVHDEPYN YPGTNTPVYN WDRGYFGNIT
LQYALQQSRN VPAVETLNKV GLNRAKTFLN GLGIDYPSIH YSNAISSNTT ESDKKYGASS
EKMAAAYAAF ANGGTYYKPM YIHKVVFSDG SEKEFSNVGT RAMKETTAYM MTDMMKTVLT
YGTGRNAYLA WLPQAGKTGT SNYTDEEIEN HIKTSQFVAP DELFAGYTRK YSMAVWTGYS
NRLTPLVGNG LTVAAKVYRS MMTYLSEGSN PEDWNIPEGL YRNGEFVFKN GARSTWNSPA
PQQPPSTESS SSSSDSSTSQ SSSTTPSTNN STTTNPNNNT QQSNTTPDQQ NQNPQPAQP
