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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_RICCN              Reviewed;         790 AA.
Q92G78;
15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
01-DEC-2001, sequence version 1.
16-JAN-2019, entry version 103.
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=RC1245;
Rickettsia conorii (strain ATCC VR-613 / Malish 7).
Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
Rickettsiaceae; Rickettsieae; Rickettsia; spotted fever group.
NCBI_TaxID=272944;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC VR-613 / Malish 7;
PubMed=11557893; DOI=10.1126/science.1061471;
Ogata H., Audic S., Renesto-Audiffren P., Fournier P.-E., Barbe V.,
Samson D., Roux V., Cossart P., Weissenbach J., Claverie J.-M.,
Raoult D.;
"Mechanisms of evolution in Rickettsia conorii and R. prowazekii.";
Science 293:2093-2098(2001).
-!- FUNCTION: Cell wall formation. Synthesis of cross-linked
peptidoglycan from the lipid intermediates. The enzyme has a
penicillin-insensitive transglycosylase N-terminal domain
(formation of linear glycan strands) and a penicillin-sensitive
transpeptidase C-terminal domain (cross-linking of the peptide
subunits). {ECO:0000250}.
-!- CATALYTIC ACTIVITY:
Reaction=[GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-
D-Ala)](n)-diphospho-di-trans,octa-cis-undecaprenol + beta-D-
GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-
diphospho-di-trans,octa-cis-undecaprenol = [GlcNAc-(1->4)-
Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)](n+1)-diphospho-
di-trans-octa-cis-undecaprenol + di-trans,octa-cis-undecaprenyl
diphosphate + H(+); Xref=Rhea:RHEA:23708, Rhea:RHEA-COMP:9602,
Rhea:RHEA-COMP:9603, ChEBI:CHEBI:15378, ChEBI:CHEBI:58405,
ChEBI:CHEBI:60033, ChEBI:CHEBI:78435; EC=2.4.1.129;
Evidence={ECO:0000250|UniProtKB:P02918};
-!- CATALYTIC ACTIVITY:
Reaction=Preferential cleavage: (Ac)(2)-L-Lys-D-Ala-|-D-Ala. Also
transpeptidation of peptidyl-alanyl moieties that are N-acyl
substituents of D-alanine.; EC=3.4.16.4;
Evidence={ECO:0000250|UniProtKB:P02918};
-!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
-!- 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; AE006914; AAL03783.1; -; Genomic_DNA.
PIR; E97855; E97855.
RefSeq; WP_010977809.1; NC_003103.1.
ProteinModelPortal; Q92G78; -.
SMR; Q92G78; -.
CAZy; GT51; Glycosyltransferase Family 51.
PRIDE; Q92G78; -.
EnsemblBacteria; AAL03783; AAL03783; RC1245.
GeneID; 928398; -.
KEGG; rco:RC1245; -.
PATRIC; fig|272944.4.peg.1427; -.
HOGENOM; HOG000041137; -.
KO; K05366; -.
OMA; LAQMAMI; -.
BioCyc; RCON272944:G1FZG-2004-MONOMER; -.
UniPathway; UPA00219; -.
Proteomes; UP000000816; Chromosome.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005886; C:plasma membrane; 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; IPR031376; PCB_OB.
InterPro; IPR001460; PCN-bd_Tpept.
Pfam; PF17092; PCB_OB; 1.
Pfam; PF00912; Transgly; 1.
Pfam; PF00905; Transpeptidase; 1.
SUPFAM; SSF53955; SSF53955; 1.
SUPFAM; SSF56601; SSF56601; 1.
3: Inferred from homology;
Antibiotic resistance; Carboxypeptidase; Cell inner membrane;
Cell membrane; Cell shape; Cell wall biogenesis/degradation;
Complete proteome; Glycosyltransferase; Hydrolase; Membrane;
Multifunctional enzyme; Peptidoglycan synthesis; Protease;
Signal-anchor; Transferase; Transmembrane; Transmembrane helix.
CHAIN 1 790 Penicillin-binding protein 1A.
/FTId=PRO_0000286451.
TOPO_DOM 1 6 Cytoplasmic. {ECO:0000255}.
TRANSMEM 7 27 Helical; Signal-anchor for type II
membrane protein. {ECO:0000255}.
TOPO_DOM 28 790 Periplasmic. {ECO:0000255}.
REGION 49 220 Transglycosylase.
REGION 398 711 Transpeptidase.
ACT_SITE 87 87 Proton donor; for transglycosylase
activity. {ECO:0000250|UniProtKB:P02919}.
ACT_SITE 457 457 Acyl-ester intermediate; for
transpeptidase activity.
{ECO:0000250|UniProtKB:P02919}.
SEQUENCE 790 AA; 88684 MW; 47CDF1B83DCA8A1B CRC64;
MYKSLLFCLK IFVFLILVGC GITAYIIYHY SRDLPDYSQL ARYYPPSVTR IYSRDGKLME
EYAFERRVFV PINSVPSSLI ESFIAAEDKN FYNHPGVDLF GIVRAAFLNI SNYLHHRRME
GASTITQQVV KNFLLTNEVS LERKIKEAIL SYMISRVFTK DQILELYLNQ TFFGRGAYGV
AVAAQNYFNK SVEELTIAES AFIAALPKAP SELNPERNYA RVKARRDYVI TRMFEDGYIT
RDAAKEAMDS PIVLRKRAKE ETVTADYYAA QVREEVIRML NSKEVFYTGG LTIITSLDAK
MQQLAENSLR KGLREFDRRC GFRKPIANIS LDNWQGELKK LPTPPSLLEY KLAVVLDVAD
NHVEIGLIDG SKSKMPIAEM KWARSNFKSV KTLLKKGDVI VVEAIKEGYA LRQIPEVNGA
IMVMNPNTGQ VLASVGGYDF STSKFDRVTQ ALRQPGSLSK TFVYLAALEN GVKPNQIFND
GPIEISQGPG MPSWRPKNYE GKFLGEITMR TGLEKSRNLI TVRVATAVGL TKIVDIIKRF
GINNEPKKVY SMVLGSIETT LSRMTNAYAI IANGGKKVEP HFVELIKDRN GKIIYRRDDR
ECLACNVSDS NLDTAILEIP KEYIYRVTDE ASDYQITSFL TGAIDRGTGY AAKKLGKIIG
GKTGTSNDSK DTWFVGFTPK IVVGSYVGYD TPKELGKRAT GSNVVLPIFI DFMSNAYKDK
PSLPFKVPDS IKLIAVDSAT GKITPGGTVI EAFKVNNVQM LENEDMIDNQ DNNDIFDYVP
SKEDQSQEIY


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