ID D0S1P5_ACICA Unreviewed; 382 AA.
AC D0S1P5;
DT 15-DEC-2009, integrated into UniProtKB/TrEMBL.
DT 15-DEC-2009, sequence version 1.
DT 27-MAR-2024, entry version 48.
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 Name=dacF {ECO:0000313|EMBL:EEY77362.1};
GN ORFNames=HMPREF0012_00231 {ECO:0000313|EMBL:EEY77362.1};
OS Acinetobacter calcoaceticus RUH2202.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Acinetobacter; Acinetobacter calcoaceticus/baumannii complex.
OX NCBI_TaxID=575585 {ECO:0000313|EMBL:EEY77362.1, ECO:0000313|Proteomes:UP000005126};
RN [1] {ECO:0000313|Proteomes:UP000005126}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RUH2202 {ECO:0000313|Proteomes:UP000005126};
RX PubMed=23144699; DOI=10.1371/journal.pone.0046984;
RA Peleg A.Y., de Breij A., Adams M.D., Cerqueira G.M., Mocali S.,
RA Galardini M., Nibbering P.H., Earl A.M., Ward D.V., Paterson D.L.,
RA Seifert H., Dijkshoorn L.;
RT "The success of Acinetobacter species; genetic, metabolic and virulence
RT attributes.";
RL PLoS ONE 7:E46984-E46984(2012).
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}.
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DR EMBL; GG704949; EEY77362.1; -; Genomic_DNA.
DR RefSeq; WP_003650463.1; NZ_GG704949.1.
DR AlphaFoldDB; D0S1P5; -.
DR HOGENOM; CLU_027070_8_1_6; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000005126; 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:EEY77362.1}; Cell shape {ECO:0000256|ARBA:ARBA00022960};
KW Cell wall biogenesis/degradation {ECO:0000256|ARBA:ARBA00023316};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:EEY77362.1};
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_5003015628"
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; 41683 MW; D76F4D35B2839C43 CRC64;
MTRKSAIAAL LLLPSFSYAA TVLSAPPELN NKSYVLMDYE TGQILASKNE NEKLAPASMT
KMMTSYIIEQ KLLKGDLTEN EQVRMNESAW CKGSSSESCM YVPLNGTATV LEMLRGIIIQ
SGNDASKAMA EHIAGNEGTF AHMMNQEAKR IGMVNTQFVN STGMPAEGHY STAKDMAVLA
QHIIKDSSKY YPIYSEKEFT FNGIKQGNRN ALLYTDPSVD GLKTGHTDEA GYCLTTSSKR
GPMRLVSVIF GTPSMAERAD QTRALLAWGF ANFETANVQP ANQVLAKAKV WFGKEDEVQV
GLAENFSVTM PKGKADGIKT QLVVQPNLNA PLQKGQVVGK LVASLDGKVI AEKPLVALKP
VEEAGFFARL IDHVKQFFSN LF
//
