ID X0PKV5_9LACO Unreviewed; 550 AA.
AC X0PKV5;
DT 14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT 14-MAY-2014, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE SubName: Full=Amidohydrolase 3 {ECO:0000313|EMBL:KRM11196.1};
DE SubName: Full=Exoenzyme regulatory protein AepA {ECO:0000313|EMBL:GAF37977.1};
GN ORFNames=FD41_GL001607 {ECO:0000313|EMBL:KRM11196.1}, JCM14108_3068
GN {ECO:0000313|EMBL:GAF37977.1};
OS Lentilactobacillus farraginis DSM 18382 = JCM 14108.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Lentilactobacillus.
OX NCBI_TaxID=1423743 {ECO:0000313|EMBL:GAF37977.1, ECO:0000313|Proteomes:UP000019488};
RN [1] {ECO:0000313|EMBL:GAF37977.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 14108 {ECO:0000313|EMBL:GAF37977.1};
RA Yuki M., Oshima K., Suda W., Kitahara M., Kitamura K., Iida T., Hattori M.,
RA Ohkuma M.;
RT "Draft Genome Sequences of Two Lactobacillus Strains, L. farraginis JCM
RT 14108T and L. composti JCM 14202T, Isolated from Compost of Distilled
RT Shochu Residue.";
RL Genome Announc. 2:e00257-14(2014).
RN [2] {ECO:0000313|EMBL:KRM11196.1, ECO:0000313|Proteomes:UP000051966}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 18382 {ECO:0000313|EMBL:KRM11196.1,
RC ECO:0000313|Proteomes:UP000051966};
RX PubMed=26415554; DOI=10.1038/ncomms9322;
RA Sun Z., Harris H.M., McCann A., Guo C., Argimon S., Zhang W., Yang X.,
RA Jeffery I.B., Cooney J.C., Kagawa T.F., Liu W., Song Y., Salvetti E.,
RA Wrobel A., Rasinkangas P., Parkhill J., Rea M.C., O'Sullivan O., Ritari J.,
RA Douillard F.P., Paul Ross R., Yang R., Briner A.E., Felis G.E.,
RA de Vos W.M., Barrangou R., Klaenhammer T.R., Caufield P.W., Cui Y.,
RA Zhang H., O'Toole P.W.;
RT "Expanding the biotechnology potential of lactobacilli through comparative
RT genomics of 213 strains and associated genera.";
RL Nat. Commun. 6:8322-8322(2015).
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:GAF37977.1}.
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DR EMBL; BAKI01000059; GAF37977.1; -; Genomic_DNA.
DR EMBL; AZFY01000025; KRM11196.1; -; Genomic_DNA.
DR RefSeq; WP_035181320.1; NZ_BAKI01000059.1.
DR AlphaFoldDB; X0PKV5; -.
DR STRING; 1423743.FD41_GL001607; -.
DR PATRIC; fig|1423743.5.peg.1665; -.
DR eggNOG; COG1574; Bacteria.
DR OrthoDB; 9767366at2; -.
DR Proteomes; UP000019488; Unassembled WGS sequence.
DR Proteomes; UP000051966; Unassembled WGS sequence.
DR GO; GO:0016810; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds; IEA:InterPro.
DR CDD; cd01300; YtcJ_like; 1.
DR Gene3D; 3.10.310.70; -; 1.
DR Gene3D; 3.20.20.140; Metal-dependent hydrolases; 1.
DR Gene3D; 2.30.40.10; Urease, subunit C, domain 1; 1.
DR InterPro; IPR013108; Amidohydro_3.
DR InterPro; IPR011059; Metal-dep_hydrolase_composite.
DR InterPro; IPR032466; Metal_Hydrolase.
DR InterPro; IPR033932; YtcJ-like.
DR PANTHER; PTHR22642:SF25; EXOENZYMES REGULATORY PROTEIN; 1.
DR PANTHER; PTHR22642; IMIDAZOLONEPROPIONASE; 1.
DR Pfam; PF07969; Amidohydro_3; 1.
DR SUPFAM; SSF51338; Composite domain of metallo-dependent hydrolases; 1.
DR SUPFAM; SSF51556; Metallo-dependent hydrolases; 1.
PE 4: Predicted;
KW Hydrolase {ECO:0000313|EMBL:KRM11196.1}.
FT DOMAIN 56..536
FT /note="Amidohydrolase 3"
FT /evidence="ECO:0000259|Pfam:PF07969"
SQ SEQUENCE 550 AA; 61253 MW; 940B53CFA5B8D3B4 CRC64;
MTSIQILKSR SIFMAEAQKF IAGAVVIVDK KIAGVYSGKV PIRFLALRPK ISDFGEQTVV
PGFIESHSHM FLSALVYNQK ITLISGNSET ACAADLSSKV PRNRLKPHQW IVAKGWYVPA
WQEKRLPSRL TLDHYFPDNP VAIIADDLHT LWLNTAALDI LLPLVNPNRF DRDVTVTARG
DPSGVVGEQT AMAFLHRIFD YSNSQKAAIL APYLDHLTSL GLTSTCDLAL LPAQTINGLD
DQIYPAVYHE LAHQNRLPLR VHLYPYFKRG VAALKKLAAN YTTPRIRIAG GKLFFDGVTS
SYTAWMKAPY EGRKTMGMPI IPAAEMKKLI FLAQQSGIPL RIHAIGDQAI HEALIDFIAA
ERQFKNSGLV QHCLEHLETI DPVDLPLMTK SRVIASVQPS HPLLDYRTAD RYVGKRSQTM
WPFRSFDRHH IPMAFGTDSP VVTDITPMDN LYFAMTRQTL AGDPPTGWHS NQRLTLVQVL
AAQTIGAARA CGFADQIGSL TVGKLADIAV LDRNIEKTPI REIKDIQISG TMVDGNWEYR
KQPVNNTMKV
//
