ID A0A059KI78_9BURK Unreviewed; 496 AA.
AC A0A059KI78;
DT 09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT 09-JUL-2014, sequence version 1.
DT 24-JAN-2024, entry version 27.
DE SubName: Full=D-alanyl-D-alanine carboxypeptidase/D-alanyl-D-alanine-endopeptidase {ECO:0000313|EMBL:KDB50823.1};
GN ORFNames=X805_35940 {ECO:0000313|EMBL:KDB50823.1};
OS Sphaerotilus natans subsp. natans DSM 6575.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Sphaerotilaceae; Sphaerotilus.
OX NCBI_TaxID=1286631 {ECO:0000313|EMBL:KDB50823.1, ECO:0000313|Proteomes:UP000026714};
RN [1] {ECO:0000313|EMBL:KDB50823.1, ECO:0000313|Proteomes:UP000026714}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 6575 {ECO:0000313|EMBL:KDB50823.1,
RC ECO:0000313|Proteomes:UP000026714};
RX PubMed=24965827; DOI=10.1111/1574-6941.12372;
RA Park S., Kim D.H., Lee J.H., Hur H.G.;
RT "Sphaerotilus natans encrusted with nanoball-shaped Fe(III) oxide minerals
RT formed by nitrate-reducing mixotrophic Fe(II) oxidation.";
RL FEMS Microbiol. Ecol. 90:68-77(2014).
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:KDB50823.1}.
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DR EMBL; AZRA01000110; KDB50823.1; -; Genomic_DNA.
DR RefSeq; WP_051632227.1; NZ_AZRA01000110.1.
DR AlphaFoldDB; A0A059KI78; -.
DR STRING; 34103.SAMN05421778_102178; -.
DR MEROPS; S13.003; -.
DR PATRIC; fig|1286631.3.peg.3508; -.
DR eggNOG; COG2027; Bacteria.
DR Proteomes; UP000026714; Unassembled WGS sequence.
DR GO; GO:0004185; F:serine-type carboxypeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR Gene3D; 3.40.710.10; DD-peptidase/beta-lactamase superfamily; 2.
DR InterPro; IPR012338; Beta-lactam/transpept-like.
DR InterPro; IPR000667; Peptidase_S13.
DR NCBIfam; TIGR00666; PBP4; 1.
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.
PE 3: Inferred from homology;
KW Carboxypeptidase {ECO:0000313|EMBL:KDB50823.1};
KW Hydrolase {ECO:0000313|EMBL:KDB50823.1};
KW Protease {ECO:0000313|EMBL:KDB50823.1}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..33
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 34..496
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5001579582"
SQ SEQUENCE 496 AA; 52375 MW; 7ED2BA5D99FEC45A CRC64;
MPALPSTRLR AGLRPLLTVL PLLLAATSCS VQAEPAATSV EALPAGVRAA LERARIEPGA
LSAWVAPAEG GEARLALRPA EMAAPASVMK LVTGIAALDR LGPVFQWPTT VLAAGPDRIL
RGSGDPRLTA ERLAPLLRQA MDAGGATIDG DLILDRSAYA LPAHDPAAFD GQPLRPYNVG
PDALMVAHRS VMLTLRPDPT RGVARIAVDL PLAGVQWPET VPLAGGDCQD WRAQLAPDFA
DLSRPRLTGS FPATCGERSW PVAFPDPLPA GFAARAIEAQ WRALGGRLQG RVREGLTPAG
ATVLTEWRSP VLPEVLRDMN KHSNNMIAQQ VLLALAPGQP AQPATFEAAR AEVQALALAR
GCREGELVID NGSGLSRQER ITPRCLGRLL QWAWRQPWMP ELLASLPVAG IETTARRMTG
ASGRAHLKTG TLDGVAAIAG YVHGDDGRRH ALVAILNHPK AGGAQARAVL DEIVRWAADD
LSRPGPHALS APKDSP
//
