SCO1_BACSU
ID SCO1_BACSU Reviewed; 193 AA.
AC P54178;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 07-JUL-2009, sequence version 2.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=SCO1 protein homolog;
DE AltName: Full=BsSco;
DE Flags: Precursor;
GN Name=ypmQ; OrderedLocusNames=BSU21750;
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 / Marburg / ATCC 6051 / DSM 10 / JCM 1465 / NBRC 13719 / NCIMB
RC 3610 / NRRL NRS-744 / VKM B-501;
RX PubMed=8969496; DOI=10.1099/13500872-142-11-3005;
RA Capuano V., Galleron N., Pujic P., Sorokin A., Ehrlich S.D.;
RT "Organization of the Bacillus subtilis 168 chromosome between kdg and the
RT attachment site of the SP beta prophage: use of long accurate PCR and yeast
RT artificial chromosomes for sequencing.";
RL Microbiology 142:3005-3015(1996).
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 SEQUENCE REVISION TO 85.
RX PubMed=19383706; DOI=10.1099/mic.0.027839-0;
RA Barbe V., Cruveiller S., Kunst F., Lenoble P., Meurice G., Sekowska A.,
RA Vallenet D., Wang T., Moszer I., Medigue C., Danchin A.;
RT "From a consortium sequence to a unified sequence: the Bacillus subtilis
RT 168 reference genome a decade later.";
RL Microbiology 155:1758-1775(2009).
RN [4]
RP FUNCTION, MUTAGENESIS OF CYS-64; CYS-68 AND HIS-154, AND SUBCELLULAR
RP LOCATION.
RX PubMed=10837475; DOI=10.1074/jbc.m002741200;
RA Mattatall N.R., Jazairi J., Hill B.C.;
RT "Characterization of YpmQ, an accessory protein required for the expression
RT of cytochrome c oxidase in Bacillus subtilis.";
RL J. Biol. Chem. 275:28802-28809(2000).
RN [5]
RP SUBCELLULAR LOCATION, AND MASS SPECTROMETRY.
RX PubMed=14680962; DOI=10.1016/j.pep.2003.08.012;
RA Andrews D., Rattenbury J., Anand V., Mattatall N.R., Hill B.C.;
RT "Expression, purification, and characterization of BsSco, an accessory
RT protein involved in the assembly of cytochrome c oxidase in Bacillus
RT subtilis.";
RL Protein Expr. Purif. 33:57-65(2004).
RN [6]
RP STRUCTURE BY NMR OF 24-193, AND COPPER BINDING.
RX PubMed=14604533; DOI=10.1016/j.str.2003.10.004;
RA Balatri E., Banci L., Bertini I., Cantini F., Ciofi-Baffoni S.;
RT "Solution structure of Sco1: a thioredoxin-like protein involved in
RT cytochrome c oxidase assembly.";
RL Structure 11:1431-1443(2003).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 20-193, FUNCTION, SUBUNIT, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=15723536; DOI=10.1021/bi0480537;
RA Ye Q., Imriskova-Sosova I., Hill B.C., Jia Z.;
RT "Identification of a disulfide switch in BsSco, a member of the Sco family
RT of cytochrome c oxidase assembly proteins.";
RL Biochemistry 44:2934-2942(2005).
CC -!- FUNCTION: Necessary for insertion of copper into the active site of
CC cytochrome c oxidase. May play a role in copper homeostasis or redox
CC signaling. {ECO:0000269|PubMed:10837475, ECO:0000269|PubMed:15723536}.
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:15723536}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:10837475,
CC ECO:0000269|PubMed:14680962}; Lipid-anchor
CC {ECO:0000269|PubMed:10837475, ECO:0000269|PubMed:14680962}; Cytoplasmic
CC side {ECO:0000269|PubMed:10837475, ECO:0000269|PubMed:14680962}.
CC -!- MASS SPECTROMETRY: Mass=21108; Mass_error=64.5; Method=MALDI; Note=The
CC measured mass is closest to that of the mature protein with 2 palmitate
CC moieties.; Evidence={ECO:0000269|PubMed:14680962};
CC -!- SIMILARITY: Belongs to the SCO1/2 family. {ECO:0000305}.
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DR EMBL; L77246; AAA96641.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB14093.2; -; Genomic_DNA.
DR PIR; H69938; H69938.
DR RefSeq; NP_390058.2; NC_000964.3.
DR RefSeq; WP_003245947.1; NZ_JNCM01000036.1.
DR PDB; 1ON4; NMR; -; A=24-193.
DR PDB; 1XZO; X-ray; 1.70 A; A/B=22-193.
DR PDBsum; 1ON4; -.
DR PDBsum; 1XZO; -.
DR AlphaFoldDB; P54178; -.
DR BMRB; P54178; -.
DR SMR; P54178; -.
DR STRING; 224308.BSU21750; -.
DR PaxDb; P54178; -.
DR PRIDE; P54178; -.
DR EnsemblBacteria; CAB14093; CAB14093; BSU_21750.
DR GeneID; 939098; -.
DR KEGG; bsu:BSU21750; -.
DR PATRIC; fig|224308.179.peg.2376; -.
DR eggNOG; COG1999; Bacteria.
DR InParanoid; P54178; -.
DR OMA; MIHTENF; -.
DR PhylomeDB; P54178; -.
DR BioCyc; BSUB:BSU21750-MON; -.
DR EvolutionaryTrace; P54178; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd02968; SCO; 1.
DR InterPro; IPR003782; SCO1/SenC.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR013766; Thioredoxin_domain.
DR PANTHER; PTHR12151; PTHR12151; 1.
DR Pfam; PF02630; SCO1-SenC; 1.
DR SUPFAM; SSF52833; SSF52833; 1.
DR PROSITE; PS51352; THIOREDOXIN_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell membrane; Chaperone; Copper; Lipoprotein; Membrane;
KW Metal-binding; Palmitate; Reference proteome; Signal.
FT SIGNAL 1..18
FT /evidence="ECO:0000305"
FT CHAIN 19..193
FT /note="SCO1 protein homolog"
FT /id="PRO_0000173875"
FT DOMAIN 26..191
FT /note="Thioredoxin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT BINDING 64
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000250"
FT BINDING 68
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000250"
FT BINDING 154
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000250"
FT LIPID 19
FT /note="N-palmitoyl cysteine"
FT /evidence="ECO:0000305"
FT LIPID 19
FT /note="S-diacylglycerol cysteine"
FT /evidence="ECO:0000305"
FT MUTAGEN 64
FT /note="C->S: Abolishes cytochrome c oxidase assembly."
FT /evidence="ECO:0000269|PubMed:10837475"
FT MUTAGEN 68
FT /note="C->S: Abolishes cytochrome c oxidase assembly."
FT /evidence="ECO:0000269|PubMed:10837475"
FT MUTAGEN 154
FT /note="H->A: Abolishes cytochrome c oxidase assembly."
FT /evidence="ECO:0000269|PubMed:10837475"
FT CONFLICT 85
FT /note="E -> G (in Ref. 1; AAA96641)"
FT /evidence="ECO:0000305"
FT STRAND 36..38
FT /evidence="ECO:0007829|PDB:1XZO"
FT STRAND 44..46
FT /evidence="ECO:0007829|PDB:1XZO"
FT HELIX 48..50
FT /evidence="ECO:0007829|PDB:1XZO"
FT STRAND 55..60
FT /evidence="ECO:0007829|PDB:1XZO"
FT HELIX 71..84
FT /evidence="ECO:0007829|PDB:1XZO"
FT STRAND 90..96
FT /evidence="ECO:0007829|PDB:1XZO"
FT TURN 98..100
FT /evidence="ECO:0007829|PDB:1XZO"
FT HELIX 103..110
FT /evidence="ECO:0007829|PDB:1XZO"
FT TURN 111..114
FT /evidence="ECO:0007829|PDB:1ON4"
FT HELIX 117..119
FT /evidence="ECO:0007829|PDB:1XZO"
FT STRAND 120..124
FT /evidence="ECO:0007829|PDB:1XZO"
FT HELIX 128..139
FT /evidence="ECO:0007829|PDB:1XZO"
FT STRAND 144..146
FT /evidence="ECO:0007829|PDB:1ON4"
FT TURN 149..152
FT /evidence="ECO:0007829|PDB:1ON4"
FT STRAND 157..161
FT /evidence="ECO:0007829|PDB:1XZO"
FT STRAND 165..176
FT /evidence="ECO:0007829|PDB:1XZO"
FT HELIX 179..189
FT /evidence="ECO:0007829|PDB:1XZO"
SQ SEQUENCE 193 AA; 21718 MW; D2C57D908B4864D1 CRC64;
MKVIKGLTAG LIFLFLCACG GQQIKDPLNY EVEPFTFQNQ DGKNVSLESL KGEVWLADFI
FTNCETICPP MTAHMTDLQK KLKAENIDVR IISFSVDPEN DKPKQLKKFA ANYPLSFDNW
DFLTGYSQSE IEEFALKSFK AIVKKPEGED QVIHQSSFYL VGPDGKVLKD YNGVENTPYD
DIISDVKSAS TLK
