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Database: UniProt
Entry: A0A139NJI4_9STRE
LinkDB: A0A139NJI4_9STRE
Original site: A0A139NJI4_9STRE 
ID   A0A139NJI4_9STRE        Unreviewed;       425 AA.
AC   A0A139NJI4;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   24-JAN-2024, entry version 20.
DE   RecName: Full=serine-type D-Ala-D-Ala carboxypeptidase {ECO:0000256|ARBA:ARBA00012448};
DE            EC=3.4.16.4 {ECO:0000256|ARBA:ARBA00012448};
GN   ORFNames=STRDD12_01109 {ECO:0000313|EMBL:KXT75997.1};
OS   Streptococcus sp. DD12.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=1777880 {ECO:0000313|EMBL:KXT75997.1, ECO:0000313|Proteomes:UP000070638};
RN   [1] {ECO:0000313|EMBL:KXT75997.1, ECO:0000313|Proteomes:UP000070638}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DD12 {ECO:0000313|EMBL:KXT75997.1,
RC   ECO:0000313|Proteomes:UP000070638};
RA   Denapaite D., Rieger M., Koendgen S., Brueckner R., Ochigava I.,
RA   Kappeler P., Maetz-Rensing K., Leendertz F., Hakenbeck R.;
RT   "Highly variable Streptococcus oralis are common among viridans
RT   streptococci isolated from primates.";
RL   Submitted (JAN-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Removes C-terminal D-alanyl residues from sugar-peptide cell
CC       wall precursors. {ECO:0000256|ARBA:ARBA00003217}.
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:0000256|ARBA:ARBA00034000};
CC   -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC       {ECO:0000256|ARBA:ARBA00004752}.
CC   -!- SIMILARITY: Belongs to the peptidase S11 family.
CC       {ECO:0000256|ARBA:ARBA00007164, ECO:0000256|RuleBase:RU004016}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KXT75997.1}.
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DR   EMBL; LQRG01000010; KXT75997.1; -; Genomic_DNA.
DR   RefSeq; WP_066915919.1; NZ_KQ969495.1.
DR   AlphaFoldDB; A0A139NJI4; -.
DR   STRING; 1777880.STRDD12_01109; -.
DR   PATRIC; fig|1777880.3.peg.1139; -.
DR   OrthoDB; 9791132at2; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000070638; Unassembled WGS sequence.
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   Gene3D; 2.60.410.10; D-Ala-D-Ala carboxypeptidase, C-terminal domain; 1.
DR   Gene3D; 3.40.710.10; DD-peptidase/beta-lactamase superfamily; 1.
DR   InterPro; IPR012338; Beta-lactam/transpept-like.
DR   InterPro; IPR015956; Peniciliin-bd_prot_C_sf.
DR   InterPro; IPR018044; Peptidase_S11.
DR   InterPro; IPR012907; Peptidase_S11_C.
DR   InterPro; IPR037167; Peptidase_S11_C_sf.
DR   InterPro; IPR001967; Peptidase_S11_N.
DR   NCBIfam; NF038273; strep_PBP3; 1.
DR   PANTHER; PTHR21581; D-ALANYL-D-ALANINE CARBOXYPEPTIDASE; 1.
DR   PANTHER; PTHR21581:SF11; D-ALANYL-D-ALANINE CARBOXYPEPTIDASE DACA; 1.
DR   Pfam; PF07943; PBP5_C; 1.
DR   Pfam; PF00768; Peptidase_S11; 1.
DR   PRINTS; PR00725; DADACBPTASE1.
DR   SMART; SM00936; PBP5_C; 1.
DR   SUPFAM; SSF56601; beta-lactamase/transpeptidase-like; 1.
DR   SUPFAM; SSF69189; Penicillin-binding protein associated domain; 1.
PE   3: Inferred from homology;
KW   Carboxypeptidase {ECO:0000256|ARBA:ARBA00022645,
KW   ECO:0000313|EMBL:KXT75997.1}; Cell shape {ECO:0000256|ARBA:ARBA00022960};
KW   Cell wall biogenesis/degradation {ECO:0000256|ARBA:ARBA00023316};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:KXT75997.1};
KW   Peptidoglycan synthesis {ECO:0000256|ARBA:ARBA00022984};
KW   Protease {ECO:0000256|ARBA:ARBA00022670};
KW   Reference proteome {ECO:0000313|Proteomes:UP000070638};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..26
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           27..425
FT                   /note="serine-type D-Ala-D-Ala carboxypeptidase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5007488168"
FT   DOMAIN          298..397
FT                   /note="Peptidase S11 D-Ala-D-Ala carboxypeptidase A C-
FT                   terminal"
FT                   /evidence="ECO:0000259|SMART:SM00936"
FT   ACT_SITE        60
FT                   /note="Acyl-ester intermediate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT   ACT_SITE        63
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT   ACT_SITE        123
FT                   /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT   BINDING         244
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR618044-2"
SQ   SEQUENCE   425 AA;  45853 MW;  50692F33380A63C3 CRC64;
     MNYLSKTLYA LLASLAFLLT GLTVQADDFN AAASHAIAVE ASTGKILYEK DATSTAGIAS
     ITKILTVYLV YKQIDEGKLK WDDQVAISDY AYNLTANSDA SNVPMEARSY SVKQLVDAAM
     IASANSAAIA LAEKIGGSET KFVDMMTAQL KSWGITDARL VNASGLNNSY LGSNIYPGSS
     ASDENTMSAL DVAIIARHLI TDYPDVLKIT SQTSMDFDGS TTLQTYNEML SGMSYTREGV
     DGLKTGTTEL AGASFVATTT ENGMRIITVI LHADDADNNT MARFSATNDL MNYVYSTWQL
     QTLLKKGASY NKSQAKITDG KQASVAAVAQ NDFKVVTRKN ATDAPKLTLK TKTLEAPAKK
     GSSAGSLTFE DSDLVGTGYL ENARPQVKLV TKTSVKRSIF LKVWWNHFVN WVNTSLTATW
     LAFSE
//
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