ID K9XV65_STAC7 Unreviewed; 313 AA.
AC K9XV65;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE SubName: Full=Peptidase U61 LD-carboxypeptidase A {ECO:0000313|EMBL:AFZ35954.1};
GN OrderedLocusNames=Sta7437_2415 {ECO:0000313|EMBL:AFZ35954.1};
OS Stanieria cyanosphaera (strain ATCC 29371 / PCC 7437).
OC Bacteria; Cyanobacteriota; Cyanophyceae; Pleurocapsales; Dermocarpellaceae;
OC Stanieria.
OX NCBI_TaxID=111780 {ECO:0000313|EMBL:AFZ35954.1, ECO:0000313|Proteomes:UP000010473};
RN [1] {ECO:0000313|Proteomes:UP000010473}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29371 / PCC 7437 {ECO:0000313|Proteomes:UP000010473};
RX PubMed=23277585; DOI=10.1073/pnas.1217107110;
RA Shih P.M., Wu D., Latifi A., Axen S.D., Fewer D.P., Talla E., Calteau A.,
RA Cai F., Tandeau de Marsac N., Rippka R., Herdman M., Sivonen K.,
RA Coursin T., Laurent T., Goodwin L., Nolan M., Davenport K.W., Han C.S.,
RA Rubin E.M., Eisen J.A., Woyke T., Gugger M., Kerfeld C.A.;
RT "Improving the coverage of the cyanobacterial phylum using diversity-driven
RT genome sequencing.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:1053-1058(2013).
CC -!- SIMILARITY: Belongs to the peptidase S66 family.
CC {ECO:0000256|ARBA:ARBA00010233}.
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DR EMBL; CP003653; AFZ35954.1; -; Genomic_DNA.
DR RefSeq; WP_015193622.1; NC_019748.1.
DR AlphaFoldDB; K9XV65; -.
DR STRING; 111780.Sta7437_2415; -.
DR KEGG; scs:Sta7437_2415; -.
DR PATRIC; fig|111780.3.peg.2515; -.
DR eggNOG; COG1619; Bacteria.
DR HOGENOM; CLU_034346_3_1_3; -.
DR OrthoDB; 9807329at2; -.
DR Proteomes; UP000010473; 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; cd07025; Peptidase_S66; 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 Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000010473};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825}.
FT DOMAIN 21..146
FT /note="LD-carboxypeptidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02016"
FT DOMAIN 187..303
FT /note="LD-carboxypeptidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF17676"
FT ACT_SITE 128
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR028757-1"
FT ACT_SITE 218
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR028757-1"
FT ACT_SITE 288
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR028757-1"
SQ SEQUENCE 313 AA; 34673 MW; EA1EC89B5D0BDCA2 CRC64;
MAKSNSYPCQ LPPALKPGDR VTVIAPSGAL KEFEALEQGL AIWRSRGYQV QLGSNWNFRH
GYLAGDDRQR REALAQAWSD RDCQAILCVR GGYGGARLLE DWNWNSYLSE QTKTKSAWCN
SKWLVGFSDV TSLLWSLAKI GIAGAHAPVL TTLASEPEWS INRLFDCLEG RKLEPLQGKG
WGGSQTTGIL LPANLTVATH LLKTPIQPSF ESIILALEDV TEAPYRIDRM LTQWRLMRAF
TGIKGIALGR FSRCDAPVGF NSWSVEEVIR DRLSDLNIPI VSDLPFGHDG VNAALPVGQM
VQLDAEKGIL SWY
//
