ID A0A099FBP0_9RHOB Unreviewed; 388 AA.
AC A0A099FBP0;
DT 07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE SubName: Full=Amidohydrolase {ECO:0000313|EMBL:KGJ07653.1};
GN ORFNames=IC63_07775 {ECO:0000313|EMBL:KGJ07653.1};
OS Paracoccus sphaerophysae.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Paracoccus.
OX NCBI_TaxID=690417 {ECO:0000313|EMBL:KGJ07653.1, ECO:0000313|Proteomes:UP000029917};
RN [1] {ECO:0000313|EMBL:KGJ07653.1, ECO:0000313|Proteomes:UP000029917}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HAMBI 3106 {ECO:0000313|EMBL:KGJ07653.1,
RC ECO:0000313|Proteomes:UP000029917};
RA McGinnis J.M., Wolfgang W.J.;
RL Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KGJ07653.1, ECO:0000313|Proteomes:UP000029917}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HAMBI 3106 {ECO:0000313|EMBL:KGJ07653.1,
RC ECO:0000313|Proteomes:UP000029917};
RA Mingle L.A., Cole J.A., Lapierre P., Musser K.A.;
RT "Paracoccus sanguinis sp. nov., isolated from clinical specimens of New
RT York State patients.";
RL Submitted (OCT-2014) to the EMBL/GenBank/DDBJ databases.
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:KGJ07653.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; JRKS01000018; KGJ07653.1; -; Genomic_DNA.
DR RefSeq; WP_036718629.1; NZ_JRKS01000018.1.
DR AlphaFoldDB; A0A099FBP0; -.
DR STRING; 690417.IC63_07775; -.
DR OrthoDB; 9777385at2; -.
DR Proteomes; UP000029917; Unassembled WGS sequence.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR CDD; cd05666; M20_Acy1-like; 1.
DR Gene3D; 3.30.70.360; -; 1.
DR Gene3D; 3.40.630.10; Zn peptidases; 1.
DR InterPro; IPR017439; Amidohydrolase.
DR InterPro; IPR036264; Bact_exopeptidase_dim_dom.
DR InterPro; IPR002933; Peptidase_M20.
DR InterPro; IPR011650; Peptidase_M20_dimer.
DR NCBIfam; TIGR01891; amidohydrolases; 1.
DR PANTHER; PTHR11014:SF63; METALLOPEPTIDASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_6G09600)-RELATED; 1.
DR PANTHER; PTHR11014; PEPTIDASE M20 FAMILY MEMBER; 1.
DR Pfam; PF07687; M20_dimer; 1.
DR Pfam; PF01546; Peptidase_M20; 1.
DR PIRSF; PIRSF005962; Pept_M20D_amidohydro; 1.
DR SUPFAM; SSF55031; Bacterial exopeptidase dimerisation domain; 1.
DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE 4: Predicted;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:KGJ07653.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000029917}.
FT DOMAIN 188..272
FT /note="Peptidase M20 dimerisation"
FT /evidence="ECO:0000259|Pfam:PF07687"
SQ SEQUENCE 388 AA; 41548 MW; 49CDE3FAB2DB9A9F CRC64;
MPVKNRFAEM LPEITAWRRE FHENPELLYE VHRTAGRVAE LLREFGVDEV TEGIGRTGVV
GVIRGKTDTR GRVIGLRADM DALPINEITG LDYASKTPGV MHACGHDGHT AMLLGAAKYL
AETRNFDGTA VVIFQPAEEG GAGGLAMVED GLVDRWGIQE FYGMHNMPGI PVGSFAIREG
GIMAAADQFD IVVTGKGGHA AKPHECIDST LIAAQIIVAL QSIVSRNVDP LKNAVVSTCV
VQTDSTAYNV IPQVVRLKGT ARSLDPGVRA QLESGISRVS QGIAAAFGAQ VEVTYHRGYP
VTVNHPEETG HAISVARDLS ADVNTDVAPM MGGEDFSYML EQKPGAYIFV GNGDTAMVHH
PAYNFDDDAI PFGSSWYAGM VEARMPAA
//