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Database: UniProt
Entry: B4V8D7_9ACTN
LinkDB: B4V8D7_9ACTN
Original site: B4V8D7_9ACTN 
ID   B4V8D7_9ACTN            Unreviewed;       428 AA.
AC   B4V8D7;
DT   23-SEP-2008, integrated into UniProtKB/TrEMBL.
DT   23-SEP-2008, sequence version 1.
DT   24-JAN-2024, entry version 52.
DE   SubName: Full=Penicillin binding protein PbpA {ECO:0000313|EMBL:EDX24224.1};
DE   SubName: Full=Penicillin-binding protein {ECO:0000313|EMBL:AKL70958.1};
GN   ORFNames=M444_35650 {ECO:0000313|EMBL:AKL70958.1}, SSAG_04015
GN   {ECO:0000313|EMBL:EDX24224.1};
OS   Streptomyces sp. Mg1.
OG   Plasmid pSMg1-1 {ECO:0000313|EMBL:AKL70958.1,
OG   ECO:0000313|Proteomes:UP000035653}.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=465541 {ECO:0000313|EMBL:EDX24224.1, ECO:0000313|Proteomes:UP000005764};
RN   [1] {ECO:0000313|EMBL:EDX24224.1, ECO:0000313|Proteomes:UP000005764}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Mg1 {ECO:0000313|EMBL:EDX24224.1,
RC   ECO:0000313|Proteomes:UP000005764};
RG   The Broad Institute Genome Sequencing Platform;
RA   Fischbach M., Ward D., Young S., Jaffe D., Gnerre S., Berlin A., Heiman D.,
RA   Hepburn T., Sykes S., Mehta T., Alvarado L., Kodira C.D., Straight P.,
RA   Clardy J., Hung D., Kolter R., Mekalanos J., Walker S., Walsh C.T.,
RA   Lander E., Galagan J., Nusbaum C., Birren B.;
RT   "Annotation of Streptomyces sp. Mg1.";
RL   Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:AKL70958.1, ECO:0000313|Proteomes:UP000035653}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Mg1 {ECO:0000313|EMBL:AKL70958.1,
RC   ECO:0000313|Proteomes:UP000035653};
RC   PLASMID=Plasmid pSMg1-1 {ECO:0000313|Proteomes:UP000035653}, and
RC   pSMg1-1 {ECO:0000313|EMBL:AKL70958.1};
RX   PubMed=23908282;
RA   Hoefler B.C., Konganti K., Straight P.D.;
RT   "De Novo Assembly of the Streptomyces sp. Strain Mg1 Genome Using PacBio
RT   Single-Molecule Sequencing.";
RL   Genome Announc. 1:e00535-13(2013).
RN   [3] {ECO:0000313|EMBL:AKL70958.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Mg1 {ECO:0000313|EMBL:AKL70958.1};
RC   PLASMID=pSMg1-1 {ECO:0000313|EMBL:AKL70958.1};
RA   Hoefler B.C., Straight P.D.;
RL   Submitted (JUN-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the peptidase S11 family.
CC       {ECO:0000256|ARBA:ARBA00007164, ECO:0000256|RuleBase:RU004016}.
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DR   EMBL; CP011665; AKL70958.1; -; Genomic_DNA.
DR   EMBL; DS570408; EDX24224.1; -; Genomic_DNA.
DR   RefSeq; WP_008741247.1; NZ_DS570408.1.
DR   AlphaFoldDB; B4V8D7; -.
DR   KEGG; strm:M444_35650; -.
DR   PATRIC; fig|465541.12.peg.7596; -.
DR   eggNOG; COG1686; Bacteria.
DR   eggNOG; COG3115; Bacteria.
DR   HOGENOM; CLU_011372_1_0_11; -.
DR   Proteomes; UP000005764; Unassembled WGS sequence.
DR   Proteomes; UP000035653; Plasmid pSMg1-1.
DR   GO; GO:0009002; F:serine-type D-Ala-D-Ala carboxypeptidase activity; IEA:InterPro.
DR   GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR   GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.710.10; DD-peptidase/beta-lactamase superfamily; 1.
DR   InterPro; IPR012338; Beta-lactam/transpept-like.
DR   InterPro; IPR018044; Peptidase_S11.
DR   InterPro; IPR001967; Peptidase_S11_N.
DR   PANTHER; PTHR21581; D-ALANYL-D-ALANINE CARBOXYPEPTIDASE; 1.
DR   PANTHER; PTHR21581:SF32; D-ALANYL-D-ALANINE CARBOXYPEPTIDASE DACB; 1.
DR   Pfam; PF00768; Peptidase_S11; 1.
DR   PRINTS; PR00725; DADACBPTASE1.
DR   SUPFAM; SSF56601; beta-lactamase/transpeptidase-like; 1.
PE   3: Inferred from homology;
KW   Cell shape {ECO:0000256|ARBA:ARBA00022960};
KW   Cell wall biogenesis/degradation {ECO:0000256|ARBA:ARBA00023316};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Peptidoglycan synthesis {ECO:0000256|ARBA:ARBA00022984};
KW   Plasmid {ECO:0000313|EMBL:AKL70958.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000035653};
KW   Signal {ECO:0000256|ARBA:ARBA00022729}.
FT   DOMAIN          90..285
FT                   /note="Peptidase S11 D-alanyl-D-alanine carboxypeptidase A
FT                   N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00768"
FT   ACT_SITE        97
FT                   /note="Acyl-ester intermediate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT   ACT_SITE        100
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT   ACT_SITE        162
FT                   /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT   BINDING         267
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR618044-2"
SQ   SEQUENCE   428 AA;  44401 MW;  6D042F59B180E0ED CRC64;
     MLAELTNTPA PPETPRRTAV RRVKIWTPIL LALAGAVAGG QLLRPLPEPR LVASDTAYTL
     DGQFSVPWPA KGQGALRVPG SGDIGTFGEQ KPVPTASVAK VMTAYVILKS HPLRGGDPGP
     QIEIDAKAVA DGASEHESRV EGLVAGTKFS QQDMLKMLMI PSANNVARLL ARWDSGTDSE
     AAFVEKMNAA ARELGMTNTT YTDPSGLDAA TVSTAADQLK LADAVMKEEA FRAVVALPSA
     EIKGLSTPLY NNNTLLTVNG LSIRGIKTGS STPAGGALMW AAYKSVGDET PLILGTLMDQ
     HVDGPDPNGA NSLILVQANS RKIIEAVRQA LASAPTVRKG QQVGRVDDGL GGSTPLVATK
     DLNVIGVPGQ RLKLTLRPGA AKVPHTAKAG TEIGVLTIGD GEGAKSVPVA VGTELAEPSF
     TARVSRLG
//
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