PBPA_STRR6
ID PBPA_STRR6 Reviewed; 719 AA.
AC Q8DR59;
DT 16-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=Penicillin-binding protein 1A;
DE Short=PBP-1A;
DE AltName: Full=Exported protein 2;
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=pbpA;
GN Synonyms=exp2 {ECO:0000303|PubMed:7934910},
GN ponA {ECO:0000303|PubMed:1624444}; OrderedLocusNames=spr0329;
OS Streptococcus pneumoniae (strain ATCC BAA-255 / R6).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=171101;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1624444; DOI=10.1128/jb.174.13.4517-4523.1992;
RA Martin C., Briese T., Hakenbeck R.;
RT "Nucleotide sequences of genes encoding penicillin-binding proteins from
RT Streptococcus pneumoniae and Streptococcus oralis with high homology to
RT Escherichia coli penicillin-binding proteins 1a and 1b.";
RL J. Bacteriol. 174:4517-4523(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-255 / R6;
RX PubMed=11544234; DOI=10.1128/jb.183.19.5709-5717.2001;
RA Hoskins J., Alborn W.E. Jr., Arnold J., Blaszczak L.C., Burgett S.,
RA DeHoff B.S., Estrem S.T., Fritz L., Fu D.-J., Fuller W., Geringer C.,
RA Gilmour R., Glass J.S., Khoja H., Kraft A.R., Lagace R.E., LeBlanc D.J.,
RA Lee L.N., Lefkowitz E.J., Lu J., Matsushima P., McAhren S.M., McHenney M.,
RA McLeaster K., Mundy C.W., Nicas T.I., Norris F.H., O'Gara M., Peery R.B.,
RA Robertson G.T., Rockey P., Sun P.-M., Winkler M.E., Yang Y.,
RA Young-Bellido M., Zhao G., Zook C.A., Baltz R.H., Jaskunas S.R.,
RA Rosteck P.R. Jr., Skatrud P.L., Glass J.I.;
RT "Genome of the bacterium Streptococcus pneumoniae strain R6.";
RL J. Bacteriol. 183:5709-5717(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 293-369.
RC STRAIN=R6X;
RX PubMed=7934910; DOI=10.1111/j.1365-2958.1993.tb01233.x;
RA Pearce B.J., Yin Y.B., Masure H.R.;
RT "Genetic identification of exported proteins in Streptococcus pneumoniae.";
RL Mol. Microbiol. 9:1037-1050(1993).
RN [4]
RP DISRUPTION PHENOTYPE.
RC STRAIN=ATCC BAA-255 / R6;
RX PubMed=8454182; DOI=10.1111/j.1574-6968.1993.tb05954.x;
RA Kell C.M., Sharma U.K., Dowson C.G., Town C., Balganesh T.S., Spratt B.G.;
RT "Deletion analysis of the essentiality of penicillin-binding proteins 1A,
RT 2B and 2X of Streptococcus pneumoniae.";
RL FEMS Microbiol. Lett. 106:171-175(1993).
RN [5]
RP SUBUNIT.
RC STRAIN=R6 / R704;
RX PubMed=28710862; DOI=10.1111/mmi.13748;
RA Stamsaas G.A., Straume D., Ruud Winther A., Kjos M., Frantzen C.A.,
RA Haavarstein L.S.;
RT "Identification of EloR (Spr1851) as a regulator of cell elongation in
RT Streptococcus pneumoniae.";
RL Mol. Microbiol. 105:954-967(2017).
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 -!- SUBUNIT: Interacts with MreC in the elongasome.
CC {ECO:0000269|PubMed:28710862}.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- DISRUPTION PHENOTYPE: Not essential, it can be deleted.
CC {ECO:0000269|PubMed:8454182}.
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; M90527; AAA26956.1; -; Genomic_DNA.
DR EMBL; AE007317; AAK99133.1; -; Genomic_DNA.
DR PIR; A42893; A42893.
DR PIR; A97913; A97913.
DR RefSeq; NP_357923.1; NC_003098.1.
DR RefSeq; WP_001039991.1; NC_003098.1.
DR PDB; 2C5W; X-ray; 2.55 A; A=51-66, B=266-650.
DR PDB; 2C6W; X-ray; 2.61 A; A=51-66, B=267-650.
DR PDB; 2V2F; X-ray; 1.90 A; A=47-70.
DR PDB; 2ZC5; X-ray; 3.00 A; A/C=47-70.
DR PDB; 2ZC6; X-ray; 2.70 A; A/C=47-70.
DR PDBsum; 2C5W; -.
DR PDBsum; 2C6W; -.
DR PDBsum; 2V2F; -.
DR PDBsum; 2ZC5; -.
DR PDBsum; 2ZC6; -.
DR AlphaFoldDB; Q8DR59; -.
DR SMR; Q8DR59; -.
DR BioGRID; 4182173; 1.
DR STRING; 171101.spr0329; -.
DR DrugBank; DB08375; (2R)-2-[(1R)-1-[[(2Z)-2-(2-Amino-1,3-thiazol-4-yl)-2-methoxyiminoacetyl]amino]-2-oxoethyl]-5-methylidene-2H-1,3-thiazine-4-carboxylic acid.
DR DrugBank; DB01163; Amdinocillin.
DR DrugBank; DB00415; Ampicillin.
DR DrugBank; DB08795; Azidocillin.
DR DrugBank; DB01140; Cefadroxil.
DR DrugBank; DB00456; Cefalotin.
DR DrugBank; DB00493; Cefotaxime.
DR DrugBank; DB01331; Cefoxitin.
DR DrugBank; DB00567; Cephalexin.
DR DrugBank; DB03313; Cephalosporin C.
DR DrugBank; DB01147; Cloxacillin.
DR DrugBank; DB01000; Cyclacillin.
DR DrugBank; DB00485; Dicloxacillin.
DR DrugBank; DB00739; Hetacillin.
DR DrugBank; DB01603; Meticillin.
DR DrugBank; DB00607; Nafcillin.
DR DrugBank; DB00713; Oxacillin.
DR CAZy; GT51; Glycosyltransferase Family 51.
DR PRIDE; Q8DR59; -.
DR EnsemblBacteria; AAK99133; AAK99133; spr0329.
DR GeneID; 60234246; -.
DR KEGG; spr:spr0329; -.
DR PATRIC; fig|171101.6.peg.368; -.
DR eggNOG; COG0744; Bacteria.
DR HOGENOM; CLU_006354_2_5_9; -.
DR OMA; LAQMAMI; -.
DR UniPathway; UPA00219; -.
DR EvolutionaryTrace; Q8DR59; -.
DR Proteomes; UP000000586; Chromosome.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
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; -; 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;
KW Reference proteome; Secreted; Transferase.
FT CHAIN 1..719
FT /note="Penicillin-binding protein 1A"
FT /id="PRO_0000083183"
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 STRAND 54..56
FT /evidence="ECO:0007829|PDB:2C5W"
FT STRAND 62..65
FT /evidence="ECO:0007829|PDB:2C5W"
FT HELIX 270..272
FT /evidence="ECO:0007829|PDB:2C5W"
FT HELIX 273..287
FT /evidence="ECO:0007829|PDB:2C5W"
FT TURN 291..293
FT /evidence="ECO:0007829|PDB:2C5W"
FT STRAND 296..300
FT /evidence="ECO:0007829|PDB:2C5W"
FT HELIX 304..315
FT /evidence="ECO:0007829|PDB:2C5W"
FT STRAND 317..319
FT /evidence="ECO:0007829|PDB:2C5W"
FT STRAND 323..325
FT /evidence="ECO:0007829|PDB:2C6W"
FT STRAND 328..335
FT /evidence="ECO:0007829|PDB:2C5W"
FT TURN 336..338
FT /evidence="ECO:0007829|PDB:2C5W"
FT STRAND 340..345
FT /evidence="ECO:0007829|PDB:2C5W"
FT TURN 360..362
FT /evidence="ECO:0007829|PDB:2C5W"
FT HELIX 369..371
FT /evidence="ECO:0007829|PDB:2C5W"
FT HELIX 372..376
FT /evidence="ECO:0007829|PDB:2C5W"
FT HELIX 378..383
FT /evidence="ECO:0007829|PDB:2C5W"
FT STRAND 388..391
FT /evidence="ECO:0007829|PDB:2C5W"
FT STRAND 393..398
FT /evidence="ECO:0007829|PDB:2C5W"
FT STRAND 417..420
FT /evidence="ECO:0007829|PDB:2C5W"
FT HELIX 421..426
FT /evidence="ECO:0007829|PDB:2C5W"
FT HELIX 430..440
FT /evidence="ECO:0007829|PDB:2C5W"
FT HELIX 442..450
FT /evidence="ECO:0007829|PDB:2C5W"
FT TURN 451..453
FT /evidence="ECO:0007829|PDB:2C5W"
FT HELIX 461..464
FT /evidence="ECO:0007829|PDB:2C5W"
FT STRAND 474..477
FT /evidence="ECO:0007829|PDB:2C5W"
FT HELIX 480..491
FT /evidence="ECO:0007829|PDB:2C5W"
FT STRAND 494..497
FT /evidence="ECO:0007829|PDB:2C5W"
FT STRAND 500..507
FT /evidence="ECO:0007829|PDB:2C5W"
FT STRAND 512..514
FT /evidence="ECO:0007829|PDB:2C5W"
FT STRAND 519..521
FT /evidence="ECO:0007829|PDB:2C5W"
FT HELIX 525..541
FT /evidence="ECO:0007829|PDB:2C5W"
FT HELIX 545..547
FT /evidence="ECO:0007829|PDB:2C5W"
FT STRAND 555..560
FT /evidence="ECO:0007829|PDB:2C5W"
FT HELIX 565..570
FT /evidence="ECO:0007829|PDB:2C5W"
FT STRAND 578..580
FT /evidence="ECO:0007829|PDB:2C5W"
FT STRAND 582..587
FT /evidence="ECO:0007829|PDB:2C5W"
FT STRAND 589..598
FT /evidence="ECO:0007829|PDB:2C5W"
FT HELIX 608..612
FT /evidence="ECO:0007829|PDB:2C5W"
FT HELIX 613..626
FT /evidence="ECO:0007829|PDB:2C5W"
FT STRAND 627..629
FT /evidence="ECO:0007829|PDB:2C5W"
FT STRAND 640..643
FT /evidence="ECO:0007829|PDB:2C5W"
FT STRAND 646..649
FT /evidence="ECO:0007829|PDB:2C5W"
SQ SEQUENCE 719 AA; 79701 MW; 14537A7070799EE6 CRC64;
MNKPTILRLI KYLSISFLSL VIAAIVLGGG VFFYYVSKAP SLSESKLVAT TSSKIYDNKN
QLIADLGSER RVNAQANDIP TDLVKAIVSI EDHRFFDHRG IDTIRILGAF LRNLQSNSLQ
GGSALTQQLI 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 ALEYGVYEST ATIVHDEPYN YPGTNTPVYN WDRGYFGNIT
LQYALQQSRN VPAVETLNKV GLNRAKTFLN GLGIDYPSIH YSNAISSNTT ESDKKYGASS
EKMAAAYAAF ANGGTYYKPM YIHKVVFSDG SEKEFSNVGT RAMKETTAYM MTDMMKTVLS
YGTGRNAYLA WLPQAGKTGT SNYTDEEIEN HIKTSQFVAP DELFAGYTRK YSMAVWTGYS
NRLTPLVGNG LTVAAKVYRS MMTYLSEGSN PEDWNIPEGL YRNGEFVFKN GARSTWSSPA
PQQPPSTESS SSSSDSSTSQ SSSTTPSTNN STTTNPNNNT QQSNTTPDQQ NQNPQPAQP
