PBPA_RICFE
ID PBPA_RICFE Reviewed; 790 AA.
AC Q4UK08;
DT 15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 99.
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=RF_1276;
OS Rickettsia felis (strain ATCC VR-1525 / URRWXCal2) (Rickettsia azadi).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC Rickettsiaceae; Rickettsieae; Rickettsia; spotted fever group.
OX NCBI_TaxID=315456;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC VR-1525 / URRWXCal2;
RX PubMed=15984913; DOI=10.1371/journal.pbio.0030248;
RA Ogata H., Renesto P., Audic S., Robert C., Blanc G., Fournier P.-E.,
RA Parinello H., Claverie J.-M., Raoult D.;
RT "The genome sequence of Rickettsia felis identifies the first putative
RT conjugative plasmid in an obligate intracellular parasite.";
RL PLoS Biol. 3:1-12(2005).
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; CP000053; AAY62127.1; -; Genomic_DNA.
DR RefSeq; WP_011271576.1; NC_007109.1.
DR AlphaFoldDB; Q4UK08; -.
DR SMR; Q4UK08; -.
DR STRING; 315456.RF_1276; -.
DR CAZy; GT51; Glycosyltransferase Family 51.
DR EnsemblBacteria; AAY62127; AAY62127; RF_1276.
DR KEGG; rfe:RF_1276; -.
DR eggNOG; COG5009; Bacteria.
DR HOGENOM; CLU_006354_2_4_5; -.
DR OMA; LAQMAMI; -.
DR OrthoDB; 652304at2; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000008548; 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_0000286452"
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; 88742 MW; F3DF50EF4B5C9D99 CRC64;
MYKSLFFCLK IFAVLILVGC GITAYIIYHY SRDLPDYSQL ARYYPPSVTR IYSHDGKLME
EYAFERRVFV PINSIPSSLI ESFIAAEDKN FYNHPGVDLL GIVRAAFLNI SNYLHHRRME
GASTITQQVV KNFLLTNEVS LERKIKEAIL SYMISRVFTK EQILELYLNQ TFFGRGAYGV
AAAAQNYFNK SVEELTIAES AFIAALPKAP SELNPERNYA RVKARRDYVI ARMFEDGYIT
KDAAKEAMDS PIVLRKRAKE ETVTADYYAA QVREEVIRML NSKEEFYTGG LTIITSLDAK
MQQLAENSLR KGLREFDRRR GFRKPIANIP LDNWQEEIKK LPSPPSLLEY KLAVVLDVAD
NHAEIGLIDG SKSKILIAEM KWARSNLKSV KTLLKKGDVI VVEPIKDGYA LRQIPEVNGA
IMVMNPNTGQ VLASVGGYDF STSKFDRVTQ ALRQPGSLSK TFVYLAALEN GIKPNQIFND
GPIEISQGPG MPSWRPKNYE GKFLGEITMR TGLEKSCNLI TVRVATAVGL TKIVDIIKRF
GINNEPKKVY SMVLGSIETT LSRMTNAYAI IANGGKKVEP HFVELIKDRN GKIIYRRDNR
ECLSCNVSDS NLDIAILEIP KEDIYRVTDE ASDYQITSFL TGAIDRSTGY AAKKLGKIIG
GKTGTSNDSK DTWFVGFTPK IVVGSYVGYD TPKELGKRAT GSNVVLPIFI DFMSNAYKDE
PSLPFKVPDS IKLIAVDRAT GKITPSGTVI EAFKVNNIQM LENEDMIDNR DNNDIFDYVP
SKEDQSQEIY
