ID A8FEQ5_BACP2 Unreviewed; 383 AA.
AC A8FEQ5;
DT 13-NOV-2007, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 2.
DT 24-JAN-2024, entry version 80.
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 OrderedLocusNames=BPUM_2052 {ECO:0000313|EMBL:ABV62722.2};
OS Bacillus pumilus (strain SAFR-032).
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=315750 {ECO:0000313|EMBL:ABV62722.2, ECO:0000313|Proteomes:UP000001355};
RN [1] {ECO:0000313|EMBL:ABV62722.2, ECO:0000313|Proteomes:UP000001355}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SAFR-032 {ECO:0000313|EMBL:ABV62722.2,
RC ECO:0000313|Proteomes:UP000001355};
RX PubMed=17895969; DOI=10.1371/journal.pone.0000928;
RA Gioia J., Yerrapragada S., Qin X., Jiang H., Igboeli O.C., Muzny D.,
RA Dugan-Rocha S., Ding Y., Hawes A., Liu W., Perez L., Kovar C., Dinh H.,
RA Lee S., Nazareth L., Blyth P., Holder M., Buhay C., Tirumalai M.R., Liu Y.,
RA Dasgupta I., Bokhetache L., Fujita M., Karouia F., Eswara Moorthy P.,
RA Siefert J., Uzman A., Buzumbo P., Verma A., Zwiya H., McWilliams B.D.,
RA Olowu A., Clinkenbeard K.D., Newcombe D., Golebiewski L., Petrosino J.F.,
RA Nicholson W.L., Fox G.E., Venkateswaran K., Highlander S.K.,
RA Weinstock G.M.;
RT "Paradoxical DNA repair and peroxide resistance gene conservation in
RT Bacillus pumilus SAFR-032.";
RL PLoS ONE 2:E928-E928(2007).
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}.
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DR EMBL; CP000813; ABV62722.2; -; Genomic_DNA.
DR RefSeq; WP_041815679.1; NZ_VEIS01000005.1.
DR AlphaFoldDB; A8FEQ5; -.
DR STRING; 315750.BPUM_2052; -.
DR MEROPS; S11.004; -.
DR KEGG; bpu:BPUM_2052; -.
DR eggNOG; COG1686; Bacteria.
DR OrthoDB; 9791132at2; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000001355; Chromosome.
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; 2.30.140.30; -; 1.
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; IPR012907; Peptidase_S11_C.
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; PF07943; PBP5_C; 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:ABV62722.2};
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 Protease {ECO:0000256|ARBA:ARBA00022670};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..383
FT /note="serine-type D-Ala-D-Ala carboxypeptidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5039645837"
FT DOMAIN 30..251
FT /note="Peptidase S11 D-alanyl-D-alanine carboxypeptidase A
FT N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00768"
FT DOMAIN 268..355
FT /note="Peptidase S11 D-Ala-D-Ala carboxypeptidase A C-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF07943"
FT ACT_SITE 61
FT /note="Acyl-ester intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT ACT_SITE 64
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT ACT_SITE 116
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT BINDING 221
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-2"
SQ SEQUENCE 383 AA; 42999 MW; 331BFC2C0F9749B7 CRC64;
MPYLKIGTAV LLLFTLLLPF SSHAKADVSL SVSARSAILI DGQSGRVLFG KDEHEKRRIA
SITKIMTAVL AIESGKMKDT VKVSKRAIQA EGSSIYLKEG QKVSLEDLTY GLMLRSGNDA
AVAIAEHVGG SLEGFIFMMN QKASELGMEN TNFQNPHGLD DHKNHYSSAY DMAILTRYAM
EHKQYQKIAG TTFYKAKTME GYWKNKNKLL TGLYQYSTGG KTGYTKLAKR TLVSTAAKGN
AALIAVTINA PDDWKDHISM FEYAFDHYKT YVLAEKGRLA SLKGTFYEKK AFIKRDVDYF
LNEDEKKLVE IETEMLTPQK KWAKNAEAIP DVVGKMTFLL DGQVIEQVPI FYENKRNRMP
QKSFQEMFKS VFQTSIGGSS WSI
//
