ID B9XI94_PEDPL Unreviewed; 802 AA.
AC B9XI94;
DT 14-APR-2009, integrated into UniProtKB/TrEMBL.
DT 14-APR-2009, sequence version 1.
DT 24-JAN-2024, entry version 61.
DE SubName: Full=D-alanyl-D-alanine carboxypeptidase/D-alanyl-D-alanine-endopeptidase {ECO:0000313|EMBL:EEF60355.1};
DE Flags: Precursor;
GN ORFNames=Cflav_PD3325 {ECO:0000313|EMBL:EEF60355.1};
OS Pedosphaera parvula (strain Ellin514).
OC Bacteria; Verrucomicrobiota; Verrucomicrobiae; Limisphaerales; Pedosphaera.
OX NCBI_TaxID=320771 {ECO:0000313|EMBL:EEF60355.1, ECO:0000313|Proteomes:UP000003688};
RN [1] {ECO:0000313|EMBL:EEF60355.1, ECO:0000313|Proteomes:UP000003688}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ellin514 {ECO:0000313|EMBL:EEF60355.1,
RC ECO:0000313|Proteomes:UP000003688};
RX PubMed=21460084; DOI=10.1128/JB.00299-11;
RA Kant R., van Passel M.W., Sangwan P., Palva A., Lucas S., Copeland A.,
RA Lapidus A., Glavina Del Rio T., Dalin E., Tice H., Bruce D., Goodwin L.,
RA Pitluck S., Chertkov O., Larimer F.W., Land M.L., Hauser L., Brettin T.S.,
RA Detter J.C., Han S., de Vos W.M., Janssen P.H., Smidt H.;
RT "Genome sequence of 'Pedosphaera parvula' Ellin514, an aerobic
RT Verrucomicrobial isolate from pasture soil.";
RL J. Bacteriol. 193:2900-2901(2011).
CC -!- SIMILARITY: Belongs to the peptidase S13 family.
CC {ECO:0000256|ARBA:ARBA00006096}.
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:EEF60355.1}.
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DR EMBL; ABOX02000017; EEF60355.1; -; Genomic_DNA.
DR RefSeq; WP_007415538.1; NZ_ABOX02000017.1.
DR AlphaFoldDB; B9XI94; -.
DR STRING; 320771.Cflav_PD3325; -.
DR OrthoDB; 9802627at2; -.
DR Proteomes; UP000003688; Unassembled WGS sequence.
DR GO; GO:0004185; F:serine-type carboxypeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR Gene3D; 3.50.80.20; D-Ala-D-Ala carboxypeptidase C, peptidase S13; 1.
DR Gene3D; 3.40.710.10; DD-peptidase/beta-lactamase superfamily; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR InterPro; IPR012338; Beta-lactam/transpept-like.
DR InterPro; IPR036116; FN3_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR000667; Peptidase_S13.
DR PANTHER; PTHR30023; D-ALANYL-D-ALANINE CARBOXYPEPTIDASE; 1.
DR PANTHER; PTHR30023:SF0; PENICILLIN-SENSITIVE CARBOXYPEPTIDASE A; 1.
DR Pfam; PF02113; Peptidase_S13; 1.
DR PRINTS; PR00922; DADACBPTASE3.
DR SUPFAM; SSF56601; beta-lactamase/transpeptidase-like; 1.
DR SUPFAM; SSF49265; Fibronectin type III; 1.
PE 3: Inferred from homology;
KW Carboxypeptidase {ECO:0000313|EMBL:EEF60355.1};
KW Hydrolase {ECO:0000313|EMBL:EEF60355.1};
KW Protease {ECO:0000313|EMBL:EEF60355.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000003688};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..802
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002894400"
SQ SEQUENCE 802 AA; 84845 MW; 55F27A330FBE6A6B CRC64;
MKKVATLFVL LTLASFSARS TAQPIPDRID AILARAAVAT NIWSVFIQSA DGTTTDYQRN
PDTGLAPASN TKLYTSSAAW GLLGTNAAFE TRVYRNGTLS GGVLTGDLNL VSEHDITWNT
SVFSNPRAAL DRIATQLKAQ GLTSVTGNVQ CYGACFYNLA DTDPSNHDAA FQQPYNASAA
TNFVAALLAQ GITVSGIPVG KTGFTVPGTL MYTHLSTDLT YNSLPLRMDV ACTPMLKVSH
NVMADALLRH ISYKINGNDS FAAGAAQVLP WLKNVAGVST NGIAMNDGSG LSHNNKFSGR
QTVTLLRYML GTFSSYASTL PIGCVDGTLG SRFCSTDGSG QVHAKTGSLS ISIALSGYID
NKYDGRRYLF SFIANTNAID QADTRQAIDD AVVLLGARGV ALSPQLFYAA NSGSNNTILL
SWSNEKFIRT GYRVYTSADG VTFGAPINVA ANVQTYADAG LAAGTKRFYR VSVVGTNGES
PFSRVYGAQV GATPSKILIV DGYDRWQFQP SDNPKATNHS FSAIAGRSIS GPAFDTANHM
SVTNGTVPIT NYQAVIWMLG EESTQDRTFD AIEQALVTSY LNSGGNLFVS GAEVGWDLDR
TSGAATADRN FYHNQLRAVF SADDANTYAF VPLAAGIFTG NASGGFDNGT QGTYNVAYPD
VLLATNGSAA TILYSGGTGG AAAVQYDGSL GGGKVVNWGF PFETITSASV RDAYMSDVLK
FFGLISPPNI ASAKFNPVSN SISLSWSSSS GLKYRVQYKN SLTDVNWGQI GVDVVATNTV
SSIVDNGISA SPQKFYRVLM VN
//
