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Database: UniProt
Entry: PBPA_RICCN
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Original site: 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   24-JAN-2024, entry version 120.
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; Pseudomonadota; 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   GeneID; 928398; -.
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: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; Biosynthetic peptidoglycan transglycosylase-like; 1.
DR   Gene3D; 3.40.710.10; DD-peptidase/beta-lactamase superfamily; 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   NCBIfam; TIGR02074; PBP_1a_fam; 1.
DR   PANTHER; PTHR32282; BINDING PROTEIN TRANSPEPTIDASE, PUTATIVE-RELATED; 1.
DR   PANTHER; PTHR32282:SF27; PENICILLIN-BINDING PROTEIN 1A; 1.
DR   Pfam; PF17092; PCB_OB; 1.
DR   Pfam; PF00912; Transgly; 1.
DR   Pfam; PF00905; Transpeptidase; 1.
DR   SUPFAM; SSF56601; beta-lactamase/transpeptidase-like; 1.
DR   SUPFAM; SSF53955; Lysozyme-like; 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
//
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