ID A0A2G0QAH4_9GAMM Unreviewed; 333 AA.
AC A0A2G0QAH4;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE SubName: Full=Peptidase S66 {ECO:0000313|EMBL:PHM56222.1};
GN ORFNames=Xhom_01705 {ECO:0000313|EMBL:PHM56222.1};
OS Xenorhabdus hominickii.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Morganellaceae; Xenorhabdus.
OX NCBI_TaxID=351679 {ECO:0000313|EMBL:PHM56222.1, ECO:0000313|Proteomes:UP000225433};
RN [1] {ECO:0000313|EMBL:PHM56222.1, ECO:0000313|Proteomes:UP000225433}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17903 {ECO:0000313|EMBL:PHM56222.1,
RC ECO:0000313|Proteomes:UP000225433};
RX PubMed=28993611; DOI=10.1038/s41564-017-0039-9;
RA Tobias N.J., Wolff H., Djahanschiri B., Grundmann F., Kronenwerth M.,
RA Shi Y.M., Simonyi S., Grun P., Shapiro-Ilan D., Pidot S.J., Stinear T.P.,
RA Ebersberger I., Bode H.B.;
RT "Natural product diversity associated with the nematode symbionts
RT Photorhabdus and Xenorhabdus.";
RL Nat. Microbiol. 2:1676-1685(2017).
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:PHM56222.1}.
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DR EMBL; NJAI01000002; PHM56222.1; -; Genomic_DNA.
DR RefSeq; WP_069316522.1; NZ_NJAI01000002.1.
DR AlphaFoldDB; A0A2G0QAH4; -.
DR KEGG; xho:A9255_09610; -.
DR OrthoDB; 9807329at2; -.
DR Proteomes; UP000225433; 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}.
FT DOMAIN 13..132
FT /note="LD-carboxypeptidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02016"
FT DOMAIN 202..316
FT /note="LD-carboxypeptidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF17676"
FT ACT_SITE 112
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR028757-1"
FT ACT_SITE 234
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR028757-1"
FT ACT_SITE 302
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR028757-1"
SQ SEQUENCE 333 AA; 37383 MW; DD0D6AC312D84597 CRC64;
MILPPKLSIG ETIGFFSSSS PATAYAPTRF ARSVNYLERQ GYKTKAGILT GKSDFYRSGT
IMQRVEEFNA LLRDPEVRCI MSTIGGYNSN SMLPYIDYEA IKKDPKIIIG YSDITALLLG
IYNKTDVVTF YGPALVASFG EYPPLVDETF ASFSRIVSNP QSPLIYQQPK YWTDEYIEWE
DQINPKNTVP NQWTFDGKGK YRGRLIGGNL NTLNGIWGSE FMPEIKQGDI LLIEDCHQGI
EEVERALAHL HLCGIFDKVS AIILGKHEQF NDQGTGRSSL DVLKEVMNGK EVPILADFDC
CHTHPMFTMP LGVNVVIDFD SESVFLPEPW CSN
//
