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Database: UniProt
Entry: A0A0R1S6P0_9LACO
LinkDB: A0A0R1S6P0_9LACO
Original site: A0A0R1S6P0_9LACO 
ID   A0A0R1S6P0_9LACO        Unreviewed;       133 AA.
AC   A0A0R1S6P0;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   SubName: Full=Rhodanese-like protein {ECO:0000313|EMBL:KRL64615.1};
GN   ORFNames=FC85_GL001129 {ECO:0000313|EMBL:KRL64615.1};
OS   Lentilactobacillus diolivorans DSM 14421.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Lentilactobacillus.
OX   NCBI_TaxID=1423739 {ECO:0000313|EMBL:KRL64615.1, ECO:0000313|Proteomes:UP000052013};
RN   [1] {ECO:0000313|EMBL:KRL64615.1, ECO:0000313|Proteomes:UP000052013}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 14421 {ECO:0000313|EMBL:KRL64615.1,
RC   ECO:0000313|Proteomes:UP000052013};
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:KRL64615.1}.
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DR   EMBL; AZEY01000090; KRL64615.1; -; Genomic_DNA.
DR   RefSeq; WP_057865566.1; NZ_AZEY01000090.1.
DR   AlphaFoldDB; A0A0R1S6P0; -.
DR   STRING; 1423739.FC85_GL001129; -.
DR   PATRIC; fig|1423739.3.peg.1181; -.
DR   Proteomes; UP000052013; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   CDD; cd00158; RHOD; 1.
DR   Gene3D; 3.40.250.10; Rhodanese-like domain; 1.
DR   InterPro; IPR001763; Rhodanese-like_dom.
DR   InterPro; IPR036873; Rhodanese-like_dom_sf.
DR   PANTHER; PTHR43031; FAD-DEPENDENT OXIDOREDUCTASE; 1.
DR   PANTHER; PTHR43031:SF14; RHODANESE DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF00581; Rhodanese; 1.
DR   SMART; SM00450; RHOD; 1.
DR   SUPFAM; SSF52821; Rhodanese/Cell cycle control phosphatase; 1.
DR   PROSITE; PS50206; RHODANESE_3; 1.
PE   4: Predicted;
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000052013};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        6..25
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          45..129
FT                   /note="Rhodanese"
FT                   /evidence="ECO:0000259|PROSITE:PS50206"
SQ   SEQUENCE   133 AA;  15616 MW;  45905A8D0F207AE1 CRC64;
     MNNANTWMTI ILIIMILAWV GYTVVQNMRV KKVATYLTND KFQSGMRKAQ VIDLREQKSF
     KDGHILGARN LPYSTIRNFY HQIRPDLPVY LYDQGKTISK RAALYLSKKG YHELYILKTG
     YQNWNGKEKK SHN
//
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