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PBPA_RICTY
ID   PBPA_RICTY              Reviewed;         785 AA.
AC   Q68VU2;
DT   15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   03-AUG-2022, entry version 103.
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=RT0794;
OS   Rickettsia typhi (strain ATCC VR-144 / Wilmington).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC   Rickettsiaceae; Rickettsieae; Rickettsia; typhus group.
OX   NCBI_TaxID=257363;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC VR-144 / Wilmington;
RX   PubMed=15317790; DOI=10.1128/jb.186.17.5842-5855.2004;
RA   McLeod M.P., Qin X., Karpathy S.E., Gioia J., Highlander S.K., Fox G.E.,
RA   McNeill T.Z., Jiang H., Muzny D., Jacob L.S., Hawes A.C., Sodergren E.,
RA   Gill R., Hume J., Morgan M., Fan G., Amin A.G., Gibbs R.A., Hong C.,
RA   Yu X.-J., Walker D.H., Weinstock G.M.;
RT   "Complete genome sequence of Rickettsia typhi and comparison with sequences
RT   of other Rickettsiae.";
RL   J. Bacteriol. 186:5842-5855(2004).
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; AE017197; AAU04250.1; -; Genomic_DNA.
DR   RefSeq; WP_011191225.1; NC_006142.1.
DR   AlphaFoldDB; Q68VU2; -.
DR   SMR; Q68VU2; -.
DR   STRING; 257363.RT0794; -.
DR   CAZy; GT51; Glycosyltransferase Family 51.
DR   EnsemblBacteria; AAU04250; AAU04250; RT0794.
DR   KEGG; rty:RT0794; -.
DR   eggNOG; COG5009; Bacteria.
DR   HOGENOM; CLU_006354_2_4_5; -.
DR   OMA; LAQMAMI; -.
DR   OrthoDB; 652304at2; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000000604; 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..785
FT                   /note="Penicillin-binding protein 1A"
FT                   /id="PRO_0000286453"
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..785
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   785 AA;  88677 MW;  2994C9F7EFD86EF0 CRC64;
     MYKSLFFFLK IFAILILLGC SVTAYIIYHY SHDLPDYSQL VRYYPPSVTR IYSRDGKLME
     EYAFERRVFV PINNVPSSLI ESFIAAEDKN FYNHPGIDLL GIVRAAFLNI SNYLHNRRME
     GASTITQQVV KNFLLTNEVS LERKIKEVII SYMISRVFTK HQILELYLNQ TFFGRGAYGV
     AAAAQNYFNK SIEELTIAES AFIAALPKAP SELNPDKNYS RVKARRDYVI ERMFEDGYIT
     RDTMKEAIGS PIVLRKRAKE ETVTADYYAA QVREEVIKML NSKEEFYRGG LTIITSLDAQ
     MQKLAENALR KGLREFDRRH GFRKPIANIP LDHWQEALKN IPTPSSLLEY KLAVVLDVSD
     NHAKIGLIDG SKARIPIIEM QWARSNLKSV KTLLKKGDVI VVEPIKDCYA LRQIPEINGA
     IMVMNPHTGQ VLASVGGYDF STSKFDRVTQ ALRQPGSLTK TFVYLAALEN GVKPNQIFND
     GPIEIMQGPG MPSWRPKNYE GQFLGEMTMR TGFEKSRNLI TVRVATAVGL TKIVDIIKRF
     GINNEPKKVY SMVLGSIETT LSRITNAYAI IANGGKKVEP HFIELIKDRN GKIIYRRDNR
     ECFSCNILDS DLDTAILEIP KEDIYRVTDE ASDYQITSFL TGAIDSGTGY AARKLGKIIA
     GKTGTSNDSK DTWFIGFTPK IVVGSYVGYD TPKELGKKAT GSNVVLPIFI DFMNHAYKDE
     PSLPFKVPDS IKLIAVDRIT GKMIPDGTVI EAFKVNNIQM LENDYMIDNH DIFIPGISDQ
     SQEIY
 
 
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