ID A0A0S2KBP9_9GAMM Unreviewed; 343 AA.
AC A0A0S2KBP9;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=LD-carboxypeptidase {ECO:0000313|EMBL:ALO45755.1};
GN ORFNames=PS2015_1093 {ECO:0000313|EMBL:ALO45755.1};
OS Pseudohongiella spirulinae.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudohongiellaceae; Pseudohongiella.
OX NCBI_TaxID=1249552 {ECO:0000313|EMBL:ALO45755.1, ECO:0000313|Proteomes:UP000065641};
RN [1] {ECO:0000313|EMBL:ALO45755.1, ECO:0000313|Proteomes:UP000065641}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KCTC 32221 {ECO:0000313|EMBL:ALO45755.1,
RC ECO:0000313|Proteomes:UP000065641};
RA Zhang Y., Guo Z.;
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peptidase S66 family.
CC {ECO:0000256|ARBA:ARBA00010233}.
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DR EMBL; CP013189; ALO45755.1; -; Genomic_DNA.
DR RefSeq; WP_058021267.1; NZ_CP013189.1.
DR AlphaFoldDB; A0A0S2KBP9; -.
DR STRING; 1249552.PS2015_1093; -.
DR KEGG; pspi:PS2015_1093; -.
DR OrthoDB; 9807329at2; -.
DR Proteomes; UP000065641; Chromosome.
DR GO; GO:0004180; F:carboxypeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0008236; F:serine-type peptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd07062; Peptidase_S66_mccF_like; 1.
DR Gene3D; 3.40.50.10740; Class I glutamine amidotransferase-like; 1.
DR Gene3D; 3.50.30.60; LD-carboxypeptidase A C-terminal domain-like; 1.
DR InterPro; IPR027461; Carboxypeptidase_A_C_sf.
DR InterPro; IPR029062; Class_I_gatase-like.
DR InterPro; IPR027478; LdcA_N.
DR InterPro; IPR040449; Peptidase_S66_N.
DR InterPro; IPR040921; Peptidase_S66C.
DR InterPro; IPR003507; S66_fam.
DR PANTHER; PTHR30237; MURAMOYLTETRAPEPTIDE CARBOXYPEPTIDASE; 1.
DR PANTHER; PTHR30237:SF2; MUREIN TETRAPEPTIDE CARBOXYPEPTIDASE; 1.
DR Pfam; PF02016; Peptidase_S66; 1.
DR Pfam; PF17676; Peptidase_S66C; 1.
DR PIRSF; PIRSF028757; LD-carboxypeptidase; 1.
DR SUPFAM; SSF52317; Class I glutamine amidotransferase-like; 1.
DR SUPFAM; SSF141986; LD-carboxypeptidase A C-terminal domain-like; 1.
PE 3: Inferred from homology;
KW Carboxypeptidase {ECO:0000256|ARBA:ARBA00022645,
KW ECO:0000313|EMBL:ALO45755.1}; Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000065641};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825}.
FT DOMAIN 13..132
FT /note="LD-carboxypeptidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02016"
FT DOMAIN 207..329
FT /note="LD-carboxypeptidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF17676"
SQ SEQUENCE 343 AA; 38493 MW; 58B56B8A27F9404B CRC64;
MKYPEPLKKG SRVAITAFSS GIAERHEKRF QEVVRTLKQR GYDVVVGDCL KSRKKHVSAP
KEQRADELLR FLTDDNIDAV APPWGGELAM ELLPLLDFKR ISRAKPKWIF GFSDVSTIAA
SINSVVGWAT VHCSNLMDLV DTNVEPLIAN TLNHLETPVG GTFVQTGSEN HTRKWPEIET
EPLAYVVGET KTQWKWLVRP MSVDAVSGRL IGGCWDTLFH LFETPFLALS ELNSKYEEGL
LLYLENAEMS PCDLVRTIHN MQFRGVFNNV NGLILGRNLR ADSQIEDDLT YLDVLTEHLA
NKNIPVMYDV DIGHVPPNLT LINGSVAEIR LVNGQGSITQ WLK
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