PBPA_RICPR
ID PBPA_RICPR Reviewed; 787 AA.
AC Q9ZCE9;
DT 20-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 133.
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=RP807;
OS Rickettsia prowazekii (strain Madrid E).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC Rickettsiaceae; Rickettsieae; Rickettsia; typhus group.
OX NCBI_TaxID=272947;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Madrid E;
RX PubMed=9823893; DOI=10.1038/24094;
RA Andersson S.G.E., Zomorodipour A., Andersson J.O., Sicheritz-Ponten T.,
RA Alsmark U.C.M., Podowski R.M., Naeslund A.K., Eriksson A.-S., Winkler H.H.,
RA Kurland C.G.;
RT "The genome sequence of Rickettsia prowazekii and the origin of
RT mitochondria.";
RL Nature 396:133-140(1998).
CC -!- FUNCTION: Cell wall formation. Synthesis of cross-linked peptidoglycan
CC from the lipid intermediates. The enzyme has a penicillin-insensitive
CC transglycosylase N-terminal domain (formation of linear glycan strands)
CC and a penicillin-sensitive transpeptidase C-terminal domain (cross-
CC linking of the peptide subunits). {ECO:0000250}.
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: 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; AJ235273; CAA15233.1; -; Genomic_DNA.
DR PIR; A71642; A71642.
DR RefSeq; NP_221157.1; NC_000963.1.
DR RefSeq; WP_004599661.1; NC_000963.1.
DR AlphaFoldDB; Q9ZCE9; -.
DR SMR; Q9ZCE9; -.
DR STRING; 272947.RP807; -.
DR CAZy; GT51; Glycosyltransferase Family 51.
DR EnsemblBacteria; CAA15233; CAA15233; CAA15233.
DR GeneID; 57569929; -.
DR KEGG; rpr:RP807; -.
DR PATRIC; fig|272947.5.peg.843; -.
DR eggNOG; COG5009; Bacteria.
DR HOGENOM; CLU_006354_2_4_5; -.
DR OMA; LAQMAMI; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000002480; 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: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; -; 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; IPR031376; PCB_OB.
DR InterPro; IPR001460; PCN-bd_Tpept.
DR Pfam; PF17092; PCB_OB; 1.
DR Pfam; PF00912; Transgly; 1.
DR Pfam; PF00905; Transpeptidase; 1.
DR SUPFAM; SSF53955; SSF53955; 1.
DR SUPFAM; SSF56601; SSF56601; 1.
PE 3: Inferred from homology;
KW 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..787
FT /note="Penicillin-binding protein 1A"
FT /id="PRO_0000083174"
FT TOPO_DOM 1..6
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 7..27
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 28..787
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT REGION 49..220
FT /note="Transglycosylase"
FT REGION 398..711
FT /note="Transpeptidase"
FT ACT_SITE 87
FT /note="Proton donor; for transglycosylase activity"
FT /evidence="ECO:0000250|UniProtKB:P02919"
FT ACT_SITE 457
FT /note="Acyl-ester intermediate; for transpeptidase
FT activity"
FT /evidence="ECO:0000250|UniProtKB:P02919"
SQ SEQUENCE 787 AA; 88694 MW; E9BF4429D17A32D0 CRC64;
MYKSLFLCLK IFAVLILIGC SVTAYIIYHY SHDLPDYSQL ARYYPPSVTR IYSRDGKLIE
EYAFERRVFV PINNVPSSLI ESFIAAEDKN FYTHPGIDLL GIVRAAFLNI SNYLHNRRME
GASTITQQVV KNFLLTNEVS LERKIKEVII SYMISRIFTK HQILELYLNQ TFFGRGAYGV
AAAAQNYFNK SVEELTIAES AFIAALPKAP SELNPDKNYS RVKARRDYVI ERMFEDGYIT
RDTMKEAIGS PIVLRKRAKE ETVTADYYAE QVREEVIRML NSKEEFYRGG LTIITSLDAK
MQQLAENSLR KGLREFDRKS GFRKPIANIP LDNWQEELKK LPTPSSLLEY KLAVVLDVSD
NHAKIGLIDG SKAKIPIVEM QWARSNLKSV KTLLKKGDVI VVEPIKDCYA LRQIPEVNGA
IMVMNPHTGQ VLASVGGYDF STSKFDRVTQ ALRQPGSLSK TFVYLAALEN GVKPNQIFND
GPIEIIQGPG MPSWCPKNYE GQFLGDMTMR TGFEKSRNLI TVRVATAVGL TKIVDIIKRF
GINNEPKKVY SMVLGSIETT LSRITNAYAI IANGGKKVEP HFVELIQDRN GKIIYRRDNR
ECFSCNIADS DLDTAILEIP KEDIYRVTDE ASNYQITSFL TGAIDSGTGY AARKLGKIIA
GKTGTSNDSK DTWFIGFTPK IVVGSYVGYD TPKELGKKAT GSNVVLPIFI DFMNHAYKDE
PSLPFKVPDS IKLIAVDRIT GKMIPNGTVI EAFKVNNIQM LENDYMIDNH DIFDYVPGML
DQSQEIY
