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Database: UniProt
Entry: B4SGL0_PELPB
LinkDB: B4SGL0_PELPB
Original site: B4SGL0_PELPB 
ID   B4SGL0_PELPB            Unreviewed;       390 AA.
AC   B4SGL0;
DT   23-SEP-2008, integrated into UniProtKB/TrEMBL.
DT   23-SEP-2008, sequence version 1.
DT   27-MAR-2024, entry version 72.
DE   SubName: Full=Serine-type D-Ala-D-Ala carboxypeptidase {ECO:0000313|EMBL:ACF43423.1};
DE            EC=3.4.16.4 {ECO:0000313|EMBL:ACF43423.1};
DE   Flags: Precursor;
GN   OrderedLocusNames=Ppha_1148 {ECO:0000313|EMBL:ACF43423.1};
OS   Pelodictyon phaeoclathratiforme (strain DSM 5477 / BU-1).
OC   Bacteria; Chlorobiota; Chlorobiia; Chlorobiales; Chlorobiaceae;
OC   Chlorobium/Pelodictyon group; Pelodictyon.
OX   NCBI_TaxID=324925 {ECO:0000313|EMBL:ACF43423.1, ECO:0000313|Proteomes:UP000002724};
RN   [1] {ECO:0000313|EMBL:ACF43423.1, ECO:0000313|Proteomes:UP000002724}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 5477 / BU-1 {ECO:0000313|Proteomes:UP000002724};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Mikhailova N., Liu Z., Li T., Zhao F., Overmann J.,
RA   Bryant D.A., Richardson P.;
RT   "Complete sequence of Pelodictyon phaeoclathratiforme BU-1.";
RL   Submitted (JUN-2008) 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; CP001110; ACF43423.1; -; Genomic_DNA.
DR   RefSeq; WP_012507915.1; NC_011060.1.
DR   AlphaFoldDB; B4SGL0; -.
DR   STRING; 324925.Ppha_1148; -.
DR   MEROPS; S11.004; -.
DR   KEGG; pph:Ppha_1148; -.
DR   eggNOG; COG1686; Bacteria.
DR   HOGENOM; CLU_027070_7_0_10; -.
DR   OrthoDB; 9791132at2; -.
DR   Proteomes; UP000002724; Chromosome.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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-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:SF34; D-ALANYL-D-ALANINE CARBOXYPEPTIDASE DACC; 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   Carboxypeptidase {ECO:0000313|EMBL:ACF43423.1};
KW   Cell shape {ECO:0000256|ARBA:ARBA00022960};
KW   Cell wall biogenesis/degradation {ECO:0000256|ARBA:ARBA00023316};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:ACF43423.1};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Peptidoglycan synthesis {ECO:0000256|ARBA:ARBA00022984};
KW   Protease {ECO:0000313|EMBL:ACF43423.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002724};
KW   Signal {ECO:0000256|ARBA:ARBA00022729};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        32..52
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          66..288
FT                   /note="Peptidase S11 D-alanyl-D-alanine carboxypeptidase A
FT                   N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00768"
FT   ACT_SITE        92
FT                   /note="Acyl-ester intermediate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT   ACT_SITE        95
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT   ACT_SITE        147
FT                   /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT   BINDING         257
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR618044-2"
SQ   SEQUENCE   390 AA;  43403 MW;  DA25D36A2993E492 CRC64;
     MPDQILISAI FRSRKRAFCI YRKPPLSLFR QITCFVVFFV IAVTITPLFL LAQTGDDSLR
     SPFPINSYIV KERGGSKFLM AKDIEKSVSP ASLTKILTCI MAIESGRLEE DVLITKESTL
     VEPSKAGFKP GEKIRLIDLV KAAMVNSSND AAFAIAIHLS GDVESFVAAM NYRAQRIGMR
     NSRFTNPAGF DKALYAGNSS TAEDLLHLTE YAVKNPVFNQ IARLEQVVFT EQTTRKVYSL
     KTHNKLLDKY PYAVGIKTGY TSTAGRCLIA RAIKDNRDIL LVMLNAKTDR WTIAADIFDS
     VFAINRPNAD WLRQSNRRNS GVSRVGQGVY SMSKSRYQMK KKVTNGAKQG HKLKNRGVVS
     AKSLKKNRKR VARSYASVVG CHVAHDDASS
//
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