PBPA_RICCN
ID PBPA_RICCN Reviewed; 790 AA.
AC Q92G78;
DT 15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 114.
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=RC1245;
OS Rickettsia conorii (strain ATCC VR-613 / Malish 7).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC Rickettsiaceae; Rickettsieae; Rickettsia; spotted fever group.
OX NCBI_TaxID=272944;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC VR-613 / Malish 7;
RX PubMed=11557893; DOI=10.1126/science.1061471;
RA Ogata H., Audic S., Renesto-Audiffren P., Fournier P.-E., Barbe V.,
RA Samson D., Roux V., Cossart P., Weissenbach J., Claverie J.-M., Raoult D.;
RT "Mechanisms of evolution in Rickettsia conorii and R. prowazekii.";
RL Science 293:2093-2098(2001).
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; AE006914; AAL03783.1; -; Genomic_DNA.
DR PIR; E97855; E97855.
DR RefSeq; WP_010977809.1; NC_003103.1.
DR AlphaFoldDB; Q92G78; -.
DR SMR; Q92G78; -.
DR CAZy; GT51; Glycosyltransferase Family 51.
DR EnsemblBacteria; AAL03783; AAL03783; RC1245.
DR KEGG; rco:RC1245; -.
DR PATRIC; fig|272944.4.peg.1427; -.
DR HOGENOM; CLU_006354_2_4_5; -.
DR OMA; LAQMAMI; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000000816; 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; Signal-anchor; Transferase;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..790
FT /note="Penicillin-binding protein 1A"
FT /id="PRO_0000286451"
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..790
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 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
