YOJM_BACSU
ID YOJM_BACSU Reviewed; 196 AA.
AC O31851;
DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=Superoxide dismutase-like protein YojM;
DE Flags: Precursor;
GN Name=yojM; OrderedLocusNames=BSU19400;
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;
RX PubMed=9734814; DOI=10.1093/dnares/5.3.195;
RA Ghim S.-Y., Choi S.-K., Shin B.-S., Jeong Y.-M., Sorokin A., Ehrlich S.D.,
RA Park S.-H.;
RT "Sequence analysis of the Bacillus subtilis 168 chromosome region between
RT the sspC and odhA loci (184 degrees-180 degrees).";
RL DNA Res. 5:195-201(1998).
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 X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 22-196 OF MUTANT HIS-88/HIS-104 IN
RP COMPLEX WITH COPPER AND ZINC IONS, AND MUTAGENESIS OF TYR-88 AND PRO-104.
RX PubMed=16173759; DOI=10.1021/ja052790o;
RA Banci L., Benvenuti M., Bertini I., Cabelli D.E., Calderone V., Fantoni A.,
RA Mangani S., Migliardi M., Viezzoli M.S.;
RT "From an inactive prokaryotic SOD homologue to an active protein through
RT site-directed mutagenesis.";
RL J. Am. Chem. Soc. 127:13287-13292(2005).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 22-196 IN COMPLEX WITH ZINC IONS,
RP AND SUBUNIT.
RX PubMed=15897454; DOI=10.1073/pnas.0502450102;
RA Banci L., Bertini I., Calderone V., Cramaro F., Del Conte R., Fantoni A.,
RA Mangani S., Quattrone A., Viezzoli M.S.;
RT "A prokaryotic superoxide dismutase paralog lacking two Cu ligands: from
RT largely unstructured in solution to ordered in the crystal.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:7541-7546(2005).
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Note=Binds 1 zinc ion per homodimer. The zinc ion is bound between 2
CC subunits and mediates dimerization.;
CC -!- SUBUNIT: Monomer, and homodimer. Largely unstructured monomer in
CC solution. Well-ordered homodimer in the crystal.
CC {ECO:0000269|PubMed:15897454, ECO:0000269|PubMed:16173759}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|PROSITE-
CC ProRule:PRU00303}; Lipid-anchor {ECO:0000255|PROSITE-ProRule:PRU00303}.
CC -!- SIMILARITY: Belongs to the Cu-Zn superoxide dismutase family.
CC {ECO:0000305}.
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DR EMBL; AF026147; AAC17861.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB13832.1; -; Genomic_DNA.
DR PIR; B69907; B69907.
DR RefSeq; NP_389822.1; NC_000964.3.
DR RefSeq; WP_004399243.1; NZ_JNCM01000036.1.
DR PDB; 1S4I; X-ray; 1.80 A; A/B/C/D=22-196.
DR PDB; 1U3N; NMR; -; A=35-196.
DR PDB; 1XTL; X-ray; 2.00 A; A/B/C/D=22-196.
DR PDB; 1XTM; X-ray; 1.60 A; A/B=22-196.
DR PDBsum; 1S4I; -.
DR PDBsum; 1U3N; -.
DR PDBsum; 1XTL; -.
DR PDBsum; 1XTM; -.
DR AlphaFoldDB; O31851; -.
DR BMRB; O31851; -.
DR SMR; O31851; -.
DR IntAct; O31851; 19.
DR STRING; 224308.BSU19400; -.
DR PaxDb; O31851; -.
DR EnsemblBacteria; CAB13832; CAB13832; BSU_19400.
DR GeneID; 939502; -.
DR KEGG; bsu:BSU19400; -.
DR PATRIC; fig|224308.179.peg.2121; -.
DR eggNOG; COG2032; Bacteria.
DR InParanoid; O31851; -.
DR OMA; EHGFNNP; -.
DR PhylomeDB; O31851; -.
DR BioCyc; BSUB:BSU19400-MON; -.
DR EvolutionaryTrace; O31851; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005507; F:copper ion binding; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; IMP:CAFA.
DR GO; GO:0004784; F:superoxide dismutase activity; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; IMP:CAFA.
DR GO; GO:0019430; P:removal of superoxide radicals; IBA:GO_Central.
DR CDD; cd00305; Cu-Zn_Superoxide_Dismutase; 1.
DR DisProt; DP00257; -.
DR Gene3D; 2.60.40.200; -; 1.
DR InterPro; IPR032831; LPAM_2.
DR InterPro; IPR036423; SOD-like_Cu/Zn_dom_sf.
DR InterPro; IPR024134; SOD_Cu/Zn_/chaperone.
DR InterPro; IPR001424; SOD_Cu_Zn_dom.
DR PANTHER; PTHR10003; PTHR10003; 1.
DR Pfam; PF13627; LPAM_2; 1.
DR Pfam; PF00080; Sod_Cu; 1.
DR SUPFAM; SSF49329; SSF49329; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell membrane; Copper; Disulfide bond; Lipoprotein; Membrane;
KW Metal-binding; Palmitate; Reference proteome; Signal; Zinc.
FT SIGNAL 1..17
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT CHAIN 18..196
FT /note="Superoxide dismutase-like protein YojM"
FT /id="PRO_0000032842"
FT BINDING 71
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="structural; ligand shared between dimeric
FT partners"
FT BINDING 86
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000255"
FT BINDING 137
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="structural; ligand shared between dimeric
FT partners"
FT BINDING 166
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000255"
FT LIPID 18
FT /note="N-palmitoyl cysteine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT LIPID 18
FT /note="S-diacylglycerol cysteine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT DISULFID 93..186
FT MUTAGEN 88
FT /note="Y->H: Leads to copper binding and enzyme activity;
FT when associated with H-104."
FT /evidence="ECO:0000269|PubMed:16173759"
FT MUTAGEN 104
FT /note="P->H: Leads to copper binding and enzyme activity;
FT when associated with H-88."
FT /evidence="ECO:0000269|PubMed:16173759"
FT STRAND 42..49
FT /evidence="ECO:0007829|PDB:1XTM"
FT TURN 50..52
FT /evidence="ECO:0007829|PDB:1U3N"
FT STRAND 54..62
FT /evidence="ECO:0007829|PDB:1XTM"
FT STRAND 64..74
FT /evidence="ECO:0007829|PDB:1XTM"
FT STRAND 85..90
FT /evidence="ECO:0007829|PDB:1XTM"
FT TURN 91..93
FT /evidence="ECO:0007829|PDB:1U3N"
FT TURN 95..97
FT /evidence="ECO:0007829|PDB:1XTM"
FT HELIX 99..101
FT /evidence="ECO:0007829|PDB:1XTM"
FT STRAND 124..129
FT /evidence="ECO:0007829|PDB:1S4I"
FT STRAND 136..142
FT /evidence="ECO:0007829|PDB:1XTM"
FT STRAND 149..152
FT /evidence="ECO:0007829|PDB:1U3N"
FT STRAND 154..157
FT /evidence="ECO:0007829|PDB:1XTM"
FT STRAND 161..168
FT /evidence="ECO:0007829|PDB:1XTM"
FT STRAND 172..174
FT /evidence="ECO:0007829|PDB:1XTM"
FT TURN 175..179
FT /evidence="ECO:0007829|PDB:1XTM"
FT STRAND 182..189
FT /evidence="ECO:0007829|PDB:1XTM"
SQ SEQUENCE 196 AA; 20953 MW; 7C00301A62188306 CRC64;
MHRLLLLMML TALGVAGCGQ KKPPDPPNRV PEKKVVETSA FGHHVQLVNR EGKAVGFIEI
KESDDEGLDI HISANSLRPG ASLGFHIYEK GSCVRPDFES AGGPFNPLNK EHGFNNPMGH
HAGDLPNLEV GADGKVDVIM NAPDTSLKKG SKLNILDEDG SAFIIHEQAD DYLTNPSGNS
GARIVCGALL GNNEKQ
