ID   YFLN_BACSU              Reviewed;         264 AA.
AC   O34409;
DT   06-JUN-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   03-AUG-2022, entry version 108.
DE   RecName: Full=Probable metallo-hydrolase YflN;
DE            EC=3.-.-.-;
GN   Name=yflN; OrderedLocusNames=BSU07620;
OS   Bacillus subtilis (strain 168).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=224308;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=168 / AC327;
RX   PubMed=9272861; DOI=10.1016/s0378-1119(97)00130-3;
RA   Yamamoto H., Uchiyama S., Nugroho F.A., Sekiguchi J.;
RT   "Cloning and sequencing of a 35.7 kb in the 70 degree-73 degree region of
RT   the Bacillus subtilis genome reveal genes for a new two-component system,
RT   three spore germination proteins, an iron uptake system and a general
RT   stress response protein.";
RL   Gene 194:191-199(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=9384377; DOI=10.1038/36786;
RA   Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA   Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA   Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA   Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA   Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA   Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA   Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA   Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA   Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA   Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA   Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA   Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA   Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA   Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA   Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA   Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA   Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA   Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA   Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA   Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA   Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA   Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA   Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA   Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA   Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA   Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA   Yoshikawa H., Danchin A.;
RT   "The complete genome sequence of the Gram-positive bacterium Bacillus
RT   subtilis.";
RL   Nature 390:249-256(1997).
RN   [3]
RP   TRANSCRIPTIONAL REGULATION.
RC   STRAIN=168;
RX   PubMed=10972810; DOI=10.1046/j.1365-2958.2000.02055.x;
RA   Yamamoto H., Murata M., Sekiguchi J.;
RT   "The CitST two-component system regulates the expression of the Mg-citrate
RT   transporter in Bacillus subtilis.";
RL   Mol. Microbiol. 37:898-912(2000).
RN   [4]
RP   TRANSCRIPTIONAL REGULATION.
RC   STRAIN=168;
RX   PubMed=11029430; DOI=10.1128/jb.182.21.6099-6105.2000;
RA   Warner J.B., Krom B.P., Magni C., Konings W.N., Lolkema J.S.;
RT   "Catabolite repression and induction of the Mg(2+)-citrate transporter CitM
RT   of Bacillus subtilis.";
RL   J. Bacteriol. 182:6099-6105(2000).
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC       Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000250};
CC   -!- INDUCTION: Expression is under strict control of the medium
CC       composition. Induced by citrate, probably via the two-component
CC       regulatory system CitT/CitS. Repressed by rapidly metabolized carbon
CC       sources like glucose, glycerol and inositol, via the carbon catabolite
CC       repression system. Is also repressed by succinate and glutamate, albeit
CC       to a lesser extent. {ECO:0000269|PubMed:10972810,
CC       ECO:0000269|PubMed:11029430}.
CC   -!- SIMILARITY: Belongs to the metallo-beta-lactamase superfamily.
CC       {ECO:0000305}.
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DR   EMBL; D86417; BAA22307.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB12591.1; -; Genomic_DNA.
DR   PIR; D69811; D69811.
DR   RefSeq; NP_388643.1; NC_000964.3.
DR   RefSeq; WP_009966790.1; NZ_JNCM01000032.1.
DR   AlphaFoldDB; O34409; -.
DR   SMR; O34409; -.
DR   STRING; 224308.BSU07620; -.
DR   PaxDb; O34409; -.
DR   EnsemblBacteria; CAB12591; CAB12591; BSU_07620.
DR   GeneID; 936120; -.
DR   KEGG; bsu:BSU07620; -.
DR   PATRIC; fig|224308.179.peg.828; -.
DR   eggNOG; COG0491; Bacteria.
DR   InParanoid; O34409; -.
DR   OMA; PGWRWLH; -.
DR   PhylomeDB; O34409; -.
DR   BioCyc; BSUB:BSU07620-MON; -.
DR   Proteomes; UP000001570; Chromosome.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   Gene3D; 3.60.15.10; -; 1.
DR   InterPro; IPR001279; Metallo-B-lactamas.
DR   InterPro; IPR036866; RibonucZ/Hydroxyglut_hydro.
DR   Pfam; PF00753; Lactamase_B; 1.
DR   SMART; SM00849; Lactamase_B; 1.
DR   SUPFAM; SSF56281; SSF56281; 1.
PE   2: Evidence at transcript level;
KW   Hydrolase; Metal-binding; Reference proteome; Zinc.
FT   CHAIN           1..264
FT                   /note="Probable metallo-hydrolase YflN"
FT                   /id="PRO_0000049536"
FT   BINDING         80
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         82
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         84
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         85
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         169
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         188
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         188
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         241
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   264 AA;  28830 MW;  776E7045A2762939 CRC64;
     MSDPYMPLTS VRSGAGFEAA KGVHGLTVQI ANVYFIQLPS EPHSFVLIDA GMPQSAGVIV
     NEAKQRFGEG FQLKAIILTH GHFDHIGAIE EILEHWDVPV YIHSREMPYV TGKEDYPPAR
     PDSKSGLVAK LSPLFPRHSI DISSHVQALP EDGSVPFLDE WMWIATPGHT PGHISLFRDD
     GRVLVAGDAV ITVEQEKMAD VLIQKQELHG PPAYFTPDTE TAAESILKLA GLEPEALLTG
     HGIPMTGKNF RSDLTELANR LSSI