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PBPA_RICBR
ID   PBPA_RICBR              Reviewed;         791 AA.
AC   Q1RKC5;
DT   15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   16-MAY-2006, sequence version 1.
DT   03-AUG-2022, entry version 107.
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=RBE_0108;
OS   Rickettsia bellii (strain RML369-C).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC   Rickettsiaceae; Rickettsieae; Rickettsia; belli group.
OX   NCBI_TaxID=336407;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RML369-C;
RX   PubMed=16703114; DOI=10.1371/journal.pgen.0020076;
RA   Ogata H., La Scola B., Audic S., Renesto P., Blanc G., Robert C.,
RA   Fournier P.-E., Claverie J.-M., Raoult D.;
RT   "Genome sequence of Rickettsia bellii illuminates the role of amoebae in
RT   gene exchanges between intracellular pathogens.";
RL   PLoS Genet. 2:733-744(2006).
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; CP000087; ABE04189.1; -; Genomic_DNA.
DR   RefSeq; WP_011476804.1; NC_007940.1.
DR   AlphaFoldDB; Q1RKC5; -.
DR   SMR; Q1RKC5; -.
DR   STRING; 336407.RBE_0108; -.
DR   CAZy; GT51; Glycosyltransferase Family 51.
DR   EnsemblBacteria; ABE04189; ABE04189; RBE_0108.
DR   KEGG; rbe:RBE_0108; -.
DR   eggNOG; COG5009; Bacteria.
DR   HOGENOM; CLU_006354_2_4_5; -.
DR   OMA; LAQMAMI; -.
DR   OrthoDB; 652304at2; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000001951; 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..791
FT                   /note="Penicillin-binding protein 1A"
FT                   /id="PRO_0000286450"
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..791
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   791 AA;  88946 MW;  7D013204EC44294F CRC64;
     MYKSLFFCLK ILALLFLIGC GIVAYIIYYY SRDLPDYRQL ARYYPPSVTR IYSRDGKLME
     EYAFERRVFI PINSIPTSLK ESFIAAEDKN FYNHQGVDLF GIVRAAFLNI SNFLHHRRME
     GASTITQQVV KNFLLTNEVS FQRKIKEAIL SYMISRVFTK DQILELYLNQ TFFGRGAYGV
     ATAAQNYFNK SVEELTIAES AFIAALPKAP SELNPEKNYA RVKARRDYVI MRMLEDGYIT
     SDAAKEAVDS PITLRKRDQD ETVTADYYAE QVRDEVIKML GSKDEFYTSG LTIITSLDAK
     MQKFAEESLR KGLRDFDRKR GFRKAIATIS LDNWQEELKK LPTTPSLLEY KIAVVLEVTD
     TQAEIGFASG AKSKIPISEM KWAKSELKSA KKLLTKGDVI VVEPVKDYYA LRQIPEVNGA
     IMVMNPNTGQ VLTSVGGYDF FASKFDRVTQ ALRQPGSLSK TFVYLAALEN GVKPNQIFND
     GPIEISQGPG MPSWRPKNYE GKFLGPITMR TGLEKSRNLV TVRVATAVGL TKIVDIIKRF
     GINDNPQKVY SMVLGSIETT LERITNAYGI IANGGKRIKP HFVELIKDRN GKVIYRRDDR
     ECTTCNVSDN DLDNAILEIP AENIYMVTDA ASDYQITSLL TGVVDRGTAY SAKKLGKVIG
     GKTGTSNDSK DTWFIGFTPK IVVGSYVGYD TPRTLGRRAT GSSVVLPIFI DFMSNAYKDE
     PPLPFKVPDS VKLQAVDRAT GQITPSGSVM EAFKINNILI IEDDSEIIDN NHNNDVFDYV
     PTEKDQSQEI Y
 
 
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