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Penicillin-binding protein 1A (PBP-1A) (Exported protein 2) [Includes: Penicillin-insensitive transglycosylase (EC 2.4.1.129) (Peptidoglycan TGase); Penicillin-sensitive transpeptidase (EC 3.4.16.4) (DD-transpeptidase)]

 PBPA_STRR6              Reviewed;         719 AA.
Q8DR59;
16-MAY-2003, integrated into UniProtKB/Swiss-Prot.
01-MAR-2003, sequence version 1.
20-JUN-2018, entry version 106.
RecName: Full=Penicillin-binding protein 1A;
Short=PBP-1A;
AltName: Full=Exported protein 2;
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=pbpA; Synonyms=exp2; OrderedLocusNames=spr0329;
Streptococcus pneumoniae (strain ATCC BAA-255 / R6).
Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
Streptococcus.
NCBI_TaxID=171101;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=1624444; DOI=10.1128/jb.174.13.4517-4523.1992;
Martin C., Briese T., Hakenbeck R.;
"Nucleotide sequences of genes encoding penicillin-binding proteins
from Streptococcus pneumoniae and Streptococcus oralis with high
homology to Escherichia coli penicillin-binding proteins 1a and 1b.";
J. Bacteriol. 174:4517-4523(1992).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC BAA-255 / R6;
PubMed=11544234; DOI=10.1128/JB.183.19.5709-5717.2001;
Hoskins J., Alborn W.E. Jr., Arnold J., Blaszczak L.C., Burgett S.,
DeHoff B.S., Estrem S.T., Fritz L., Fu D.-J., Fuller W., Geringer C.,
Gilmour R., Glass J.S., Khoja H., Kraft A.R., Lagace R.E.,
LeBlanc D.J., Lee L.N., Lefkowitz E.J., Lu J., Matsushima P.,
McAhren S.M., McHenney M., McLeaster K., Mundy C.W., Nicas T.I.,
Norris F.H., O'Gara M., Peery R.B., Robertson G.T., Rockey P.,
Sun P.-M., Winkler M.E., Yang Y., Young-Bellido M., Zhao G.,
Zook C.A., Baltz R.H., Jaskunas S.R., Rosteck P.R. Jr., Skatrud P.L.,
Glass J.I.;
"Genome of the bacterium Streptococcus pneumoniae strain R6.";
J. Bacteriol. 183:5709-5717(2001).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 293-369.
STRAIN=R6X;
PubMed=7934910; DOI=10.1111/j.1365-2958.1993.tb01233.x;
Pearce B.J., Yin Y.B., Masure H.R.;
"Genetic identification of exported proteins in Streptococcus
pneumoniae.";
Mol. Microbiol. 9:1037-1050(1993).
-!- FUNCTION: Cell wall formation.
-!- 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.
-!- SUBCELLULAR LOCATION: Secreted.
-!- 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; M90527; AAA26956.1; -; Genomic_DNA.
EMBL; AE007317; AAK99133.1; -; Genomic_DNA.
PIR; A42893; A42893.
PIR; A97913; A97913.
RefSeq; NP_357923.1; NC_003098.1.
RefSeq; WP_001039991.1; NC_003098.1.
PDB; 2C5W; X-ray; 2.55 A; A=51-66, B=266-650.
PDB; 2C6W; X-ray; 2.61 A; A=51-66, B=267-650.
PDB; 2V2F; X-ray; 1.90 A; A=47-70.
PDB; 2ZC5; X-ray; 3.00 A; A/C=47-70.
PDB; 2ZC6; X-ray; 2.70 A; A/C=47-70.
PDBsum; 2C5W; -.
PDBsum; 2C6W; -.
PDBsum; 2V2F; -.
PDBsum; 2ZC5; -.
PDBsum; 2ZC6; -.
ProteinModelPortal; Q8DR59; -.
SMR; Q8DR59; -.
STRING; 171101.spr0329; -.
DrugBank; DB01163; Amdinocillin.
DrugBank; DB00415; Ampicillin.
DrugBank; DB08795; Azidocillin.
DrugBank; DB01140; Cefadroxil.
DrugBank; DB00456; Cefalotin.
DrugBank; DB00493; Cefotaxime.
DrugBank; DB01331; Cefoxitin.
DrugBank; DB00438; Ceftazidime.
DrugBank; DB00567; Cephalexin.
DrugBank; DB03313; Cephalosporin C.
DrugBank; DB01000; Cyclacillin.
DrugBank; DB00485; Dicloxacillin.
DrugBank; DB00739; Hetacillin.
DrugBank; DB01603; Meticillin.
DrugBank; DB00607; Nafcillin.
DrugBank; DB00713; Oxacillin.
DrugBank; DB08375; PCNOTAXIME GROUP.
CAZy; GT51; Glycosyltransferase Family 51.
PRIDE; Q8DR59; -.
EnsemblBacteria; AAK99133; AAK99133; spr0329.
GeneID; 934791; -.
KEGG; spr:spr0329; -.
PATRIC; fig|171101.6.peg.368; -.
eggNOG; ENOG4105BZ4; Bacteria.
eggNOG; COG0744; LUCA.
HOGENOM; HOG000041140; -.
KO; K05366; -.
OMA; LAQMAMI; -.
BioCyc; SPNE171101:SPR0329-MONOMER; -.
UniPathway; UPA00219; -.
EvolutionaryTrace; Q8DR59; -.
Proteomes; UP000000586; Chromosome.
GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
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; 2.
1: Evidence at protein level;
3D-structure; Antibiotic resistance; Carboxypeptidase; Cell shape;
Cell wall biogenesis/degradation; Complete proteome;
Glycosyltransferase; Hydrolase; Multifunctional enzyme;
Peptidoglycan synthesis; Protease; Reference proteome; Secreted;
Transferase.
CHAIN 1 719 Penicillin-binding protein 1A.
/FTId=PRO_0000083183.
REGION 62 223 Transglycosylase.
{ECO:0000250|UniProtKB:P02919}.
REGION 297 611 Transpeptidase.
{ECO:0000250|UniProtKB:P02919}.
COMPBIAS 654 691 Ser-rich.
ACT_SITE 91 91 Proton donor; for transglycosylase
activity. {ECO:0000250|UniProtKB:P02919}.
ACT_SITE 370 370 Acyl-ester intermediate; for
transpeptidase activity.
{ECO:0000250|UniProtKB:P02919}.
STRAND 54 56 {ECO:0000244|PDB:2C5W}.
STRAND 62 65 {ECO:0000244|PDB:2C5W}.
HELIX 270 272 {ECO:0000244|PDB:2C5W}.
HELIX 273 287 {ECO:0000244|PDB:2C5W}.
TURN 291 293 {ECO:0000244|PDB:2C5W}.
STRAND 296 300 {ECO:0000244|PDB:2C5W}.
HELIX 304 315 {ECO:0000244|PDB:2C5W}.
STRAND 317 319 {ECO:0000244|PDB:2C5W}.
STRAND 323 325 {ECO:0000244|PDB:2C6W}.
STRAND 328 335 {ECO:0000244|PDB:2C5W}.
TURN 336 338 {ECO:0000244|PDB:2C5W}.
STRAND 340 345 {ECO:0000244|PDB:2C5W}.
TURN 360 362 {ECO:0000244|PDB:2C5W}.
HELIX 369 371 {ECO:0000244|PDB:2C5W}.
HELIX 372 376 {ECO:0000244|PDB:2C5W}.
HELIX 378 383 {ECO:0000244|PDB:2C5W}.
STRAND 388 391 {ECO:0000244|PDB:2C5W}.
STRAND 393 398 {ECO:0000244|PDB:2C5W}.
STRAND 417 420 {ECO:0000244|PDB:2C5W}.
HELIX 421 426 {ECO:0000244|PDB:2C5W}.
HELIX 430 440 {ECO:0000244|PDB:2C5W}.
HELIX 442 450 {ECO:0000244|PDB:2C5W}.
TURN 451 453 {ECO:0000244|PDB:2C5W}.
HELIX 461 464 {ECO:0000244|PDB:2C5W}.
STRAND 474 477 {ECO:0000244|PDB:2C5W}.
HELIX 480 491 {ECO:0000244|PDB:2C5W}.
STRAND 494 497 {ECO:0000244|PDB:2C5W}.
STRAND 500 507 {ECO:0000244|PDB:2C5W}.
STRAND 512 514 {ECO:0000244|PDB:2C5W}.
STRAND 519 521 {ECO:0000244|PDB:2C5W}.
HELIX 525 541 {ECO:0000244|PDB:2C5W}.
HELIX 545 547 {ECO:0000244|PDB:2C5W}.
STRAND 555 560 {ECO:0000244|PDB:2C5W}.
HELIX 565 570 {ECO:0000244|PDB:2C5W}.
STRAND 578 580 {ECO:0000244|PDB:2C5W}.
STRAND 582 587 {ECO:0000244|PDB:2C5W}.
STRAND 589 598 {ECO:0000244|PDB:2C5W}.
HELIX 608 612 {ECO:0000244|PDB:2C5W}.
HELIX 613 626 {ECO:0000244|PDB:2C5W}.
STRAND 627 629 {ECO:0000244|PDB:2C5W}.
STRAND 640 643 {ECO:0000244|PDB:2C5W}.
STRAND 646 649 {ECO:0000244|PDB:2C5W}.
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


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