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Database: UniProt
Entry: A0A1X4N7Q7_9PROT
LinkDB: A0A1X4N7Q7_9PROT
Original site: A0A1X4N7Q7_9PROT 
ID   A0A1X4N7Q7_9PROT        Unreviewed;       391 AA.
AC   A0A1X4N7Q7;
DT   05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2017, 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=THS27_14830 {ECO:0000313|EMBL:OSQ42288.1};
OS   Thalassospira sp. MCCC 1A01428.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC   Thalassospiraceae; Thalassospira.
OX   NCBI_TaxID=1470575 {ECO:0000313|EMBL:OSQ42288.1, ECO:0000313|Proteomes:UP000193740};
RN   [1] {ECO:0000313|EMBL:OSQ42288.1, ECO:0000313|Proteomes:UP000193740}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MCCC 1A01428 {ECO:0000313|EMBL:OSQ42288.1,
RC   ECO:0000313|Proteomes:UP000193740};
RA   Lai Q., Shao Z.;
RT   "The draft genome sequence of Thalassospira sp. MCCC 1A01428.";
RL   Submitted (MAR-2014) 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:OSQ42288.1}.
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DR   EMBL; JFJZ01000019; OSQ42288.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1X4N7Q7; -.
DR   STRING; 1470575.THS27_14830; -.
DR   OrthoDB; 9795979at2; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000193740; 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:SF6; TRAFFICKING PROTEIN PARTICLE COMPLEX SUBUNIT 12; 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:OSQ42288.1}; 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..36
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           37..391
FT                   /note="serine-type D-Ala-D-Ala carboxypeptidase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5012869123"
FT   DOMAIN          280..370
FT                   /note="Peptidase S11 D-Ala-D-Ala carboxypeptidase A C-
FT                   terminal"
FT                   /evidence="ECO:0000259|SMART:SM00936"
FT   ACT_SITE        68
FT                   /note="Acyl-ester intermediate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT   ACT_SITE        71
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT   ACT_SITE        128
FT                   /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT   BINDING         230
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR618044-2"
SQ   SEQUENCE   391 AA;  42541 MW;  9FCF6AD4F9EE9274 CRC64;
     MNLLPSIPCK ATFNRLLAGA ALLGTVMAAT ASHAQAIDTV AREAYLVDYD TGAVLLNKNG
     DDLAEPASLT KMMTIYMLFD RIKNGSLTLK DTFHVSEDAW KKGGSKMFVE VNSDVSIYDL
     IHGIIVQSGN DAAIVVAEGI AGTEDAFAHE MTEKAREIGM TKSVFKNATG WPADGHLVTA
     HDLAVLAHRT IHDFPELYKF YSEPVFTYNG IRQHNRNPLL GTSAGVDGMK TGHTEAAGFG
     LTATAKRDGR RLILVAMGMH SMRERRTEGQ KLLDWGFREF DNYHLFKKDD VVSSADIWLG
     NAGKVDLVTD QDITLTVPRK DRKDMKVSVV YEGPIPAPIS AGQQVATLKV EIPNQDAQSF
     PLYAKSGVER LGLVGRIGAA IKYLVWGGSN G
//
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