ID H3SG67_9BACL Unreviewed; 327 AA.
AC H3SG67;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 24-JAN-2024, entry version 35.
DE RecName: Full=Peptidase U61 LD-carboxypeptidase A {ECO:0008006|Google:ProtNLM};
GN ORFNames=PDENDC454_12610 {ECO:0000313|EMBL:EHQ61877.1};
OS Paenibacillus dendritiformis C454.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=1131935 {ECO:0000313|EMBL:EHQ61877.1, ECO:0000313|Proteomes:UP000003900};
RN [1] {ECO:0000313|EMBL:EHQ61877.1, ECO:0000313|Proteomes:UP000003900}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C454 {ECO:0000313|EMBL:EHQ61877.1,
RC ECO:0000313|Proteomes:UP000003900};
RX PubMed=22461558; DOI=10.1128/JB.00158-12;
RA Sirota-Madi A., Olender T., Helman Y., Brainis I., Finkelshtein A.,
RA Roth D., Hagai E., Leshkowitz D., Brodsky L., Galatenko V., Nikolaev V.,
RA Gutnick D.L., Lancet D., Ben-Jacob E.;
RT "Genome Sequence of the Pattern-Forming Social Bacterium Paenibacillus
RT dendritiformis C454 Chiral Morphotype.";
RL J. Bacteriol. 194:2127-2128(2012).
CC -!- SIMILARITY: Belongs to the peptidase S66 family.
CC {ECO:0000256|ARBA:ARBA00010233}.
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:EHQ61877.1}.
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DR EMBL; AHKH01000028; EHQ61877.1; -; Genomic_DNA.
DR RefSeq; WP_006677021.1; NZ_AHKH01000028.1.
DR AlphaFoldDB; H3SG67; -.
DR STRING; 1131935.PDENDC454_12610; -.
DR MEROPS; S66.003; -.
DR PATRIC; fig|1131935.3.peg.2600; -.
DR OrthoDB; 9807329at2; -.
DR Proteomes; UP000003900; Unassembled WGS sequence.
DR GO; GO:0016787; F:hydrolase 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 Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Reference proteome {ECO:0000313|Proteomes:UP000003900}.
FT DOMAIN 12..131
FT /note="LD-carboxypeptidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02016"
FT DOMAIN 197..311
FT /note="LD-carboxypeptidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF17676"
FT ACT_SITE 111
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR028757-1"
FT ACT_SITE 228
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR028757-1"
FT ACT_SITE 296
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR028757-1"
SQ SEQUENCE 327 AA; 36497 MW; 4BE3BE42F4657607 CRC64;
MHAPKLKQGD EIRVIAPSRS LSLISMPQRE LAKRRLEQMG FTVTFSIHAE EMDDFISSSI
ESRVNDLHDA FRDPGVKAIL TVIGGFNSNQ LLRYLDYELI RRNPKLFCGY SDITALSNAI
YAKTGMITYS GPHFSTFGME RGIEYTAEHF LAAMTTNEVI TAKPAEQWSD DAWYRDQERR
DFILNEGWAI LQTGACEGTI IGGNVCTLNL LHGTEYMPDL QGAVLFLEDD EETDPATFDR
DLQSLLHQPG ADAVRGLVIG RFQKASRMTL DLLKQIIASK QELRGIPVIA NVDFGHTTPQ
LTFPIGGHAK LDSNPEAPLL QFGEEAF
//
