ID A0A1E8E4B0_9GAMM Unreviewed; 382 AA.
AC A0A1E8E4B0;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 30.
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=BJN41_07915 {ECO:0000313|EMBL:OFE44447.1};
OS Acinetobacter towneri.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Acinetobacter.
OX NCBI_TaxID=202956 {ECO:0000313|EMBL:OFE44447.1, ECO:0000313|Proteomes:UP000186931};
RN [1] {ECO:0000313|EMBL:OFE44447.1, ECO:0000313|Proteomes:UP000186931}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=5-2Ac02 {ECO:0000313|EMBL:OFE44447.1,
RC ECO:0000313|Proteomes:UP000186931};
RA Barbosa B., Fernandez-Garcia L., Gato E., Leao R., Albano R., Fernandez B.,
RA Fernandez-Cuenca F., Marques E., Tomas M.;
RT "Genome of airborne Acinetobacter sp. 5-2Ac02 in the hospital environment:
RT Species near to Acinetobacter towneri.";
RL Submitted (OCT-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:OFE44447.1}.
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DR EMBL; MKQS01000003; OFE44447.1; -; Genomic_DNA.
DR RefSeq; WP_070153057.1; NZ_MKQS01000003.1.
DR AlphaFoldDB; A0A1E8E4B0; -.
DR STRING; 202956.BJN41_07915; -.
DR eggNOG; COG1686; Bacteria.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000186931; 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 PANTHER; PTHR21581; D-ALANYL-D-ALANINE CARBOXYPEPTIDASE; 1.
DR PANTHER; PTHR21581:SF34; D-ALANYL-D-ALANINE CARBOXYPEPTIDASE DACC; 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:OFE44447.1}; 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..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..382
FT /note="serine-type D-Ala-D-Ala carboxypeptidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5009213429"
FT DOMAIN 273..363
FT /note="Peptidase S11 D-Ala-D-Ala carboxypeptidase A C-
FT terminal"
FT /evidence="ECO:0000259|SMART:SM00936"
FT ACT_SITE 58
FT /note="Acyl-ester intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT ACT_SITE 61
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT ACT_SITE 121
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT BINDING 223
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-2"
SQ SEQUENCE 382 AA; 42060 MW; 6FA92E34603A9B57 CRC64;
MTPKSALAAL LLLPSFSYAA TVLATPPELN NKSYVLMDYE TGQILASKNE NEKLAPASMT
KMMTSFIIEQ KLLKGELTED EQVRMNESAW CRGSSTESCM YVPLNGTATV LEMLRGIIVQ
SGNDASKAMA EHIAGNEGTF VHMMNEEAKR IGMSNTQFMN STGMPAEGHF STAKDMATLA
QHIIHDSSKY YPIYSEKEFS FNGIKQGNRN ALLYTDPSVD GLKTGHTNEA GYCLTTSAKR
GPMRLISVIF GAPTMQARAT QTRELLAWGY ANYETVRVQP ANQVLAKAKV WYGKSKEAQI
GLPENFNVTM PKGKANQIKT QLVVQPKLTA PLKKGQVIGK YVATLDGKVI AEKPLVALQE
VEEAGFFARM LDHIKQFFSN LF
//
