ID F4CCE5_SPHS2 Unreviewed; 344 AA.
AC F4CCE5;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 27-MAR-2024, entry version 52.
DE SubName: Full=Peptidase U61 LD-carboxypeptidase A {ECO:0000313|EMBL:ADZ78738.1};
GN OrderedLocusNames=Sph21_2183 {ECO:0000313|EMBL:ADZ78738.1};
OS Sphingobacterium sp. (strain 21).
OC Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC Sphingobacteriaceae; Sphingobacterium.
OX NCBI_TaxID=743722 {ECO:0000313|EMBL:ADZ78738.1};
RN [1] {ECO:0000313|EMBL:ADZ78738.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=21 {ECO:0000313|EMBL:ADZ78738.1};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Davenport K., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA Kyrpides N., Ivanova N., Ovchinnikova G., Pagani I., Siebers A.K.,
RA Allgaier M., Thelen M.P., Hugenholtz P., Woyke T.;
RT "Complete sequence of Sphingobacterium sp. 21.";
RL Submitted (MAR-2011) 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; CP002584; ADZ78738.1; -; Genomic_DNA.
DR AlphaFoldDB; F4CCE5; -.
DR STRING; 743722.Sph21_2183; -.
DR MEROPS; S66.003; -.
DR KEGG; shg:Sph21_2183; -.
DR PATRIC; fig|743722.3.peg.2332; -.
DR eggNOG; COG1619; Bacteria.
DR HOGENOM; CLU_034346_3_1_10; -.
DR GO; GO:0004180; F:carboxypeptidase activity; 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:SF5; CARBOXYPEPTIDASE YOCD-RELATED; 1.
DR PANTHER; PTHR30237; MURAMOYLTETRAPEPTIDE 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:0000313|EMBL:ADZ78738.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Protease {ECO:0000313|EMBL:ADZ78738.1}.
FT DOMAIN 35..155
FT /note="LD-carboxypeptidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02016"
FT DOMAIN 216..330
FT /note="LD-carboxypeptidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF17676"
FT ACT_SITE 135
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR028757-1"
FT ACT_SITE 247
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR028757-1"
FT ACT_SITE 315
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR028757-1"
SQ SEQUENCE 344 AA; 38382 MW; 6ADD9666E0E195B8 CRC64;
MLARPANHAL LGEVLVYKKE KQRMVVDKLK PGDHIRIIAP AQSLLPKLTQ EMRIRGVKRL
EELGLTVSFG DHVHEIDEFG STTIDNRLAD LHRAYEDKSV KAILAVSGGT TSNQLLPYID
YKLLKDNPKI LCGLSDITAL INTVYAKTDV VTYYGPHFSM LSAGEDLGFS LDYFRACLFD
DKPISLSPSP FYYNSIWEHE QLDNPGYWVI NEGDVEGKIL GGNFLTFNFL QGSEYLPDTS
DSIFFLEDNG PEDYKNVQNQ LQALLNQPSF SGVKALAIGR FKQNSMMTKE ILAKIIKTKK
QLDGIPVIAN IDFGHTLPMI TIPIGGRARV IAGPTNPVIE LLMH
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