BSHC_BACSU
ID BSHC_BACSU Reviewed; 539 AA.
AC P55342; O31722;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 16-JUN-2009, sequence version 3.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=Putative cysteine ligase BshC {ECO:0000255|HAMAP-Rule:MF_01867, ECO:0000303|PubMed:25496067};
DE EC=6.-.-.- {ECO:0000255|HAMAP-Rule:MF_01867, ECO:0000305};
GN Name=bshC {ECO:0000255|HAMAP-Rule:MF_01867, ECO:0000303|PubMed:20308541};
GN Synonyms=yllA {ECO:0000303|PubMed:8636036}; OrderedLocusNames=BSU15120;
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=8636036; DOI=10.1128/jb.178.8.2343-2350.1996;
RA Daniel R.A., Williams A.M., Errington J.;
RT "A complex four-gene operon containing essential cell division gene pbpB in
RT Bacillus subtilis.";
RL J. Bacteriol. 178:2343-2350(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 415.
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 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-131.
RC STRAIN=168;
RA Bertero M., Presecan E., Glaser P., Richou A., Danchin A.;
RT "Bacillus subtilis chromosomal region downstream nprE.";
RL Submitted (AUG-1997) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP DISRUPTION PHENOTYPE, AND PUTATIVE FUNCTION.
RC STRAIN=168;
RX PubMed=20308541; DOI=10.1073/pnas.1000928107;
RA Gaballa A., Newton G.L., Antelmann H., Parsonage D., Upton H., Rawat M.,
RA Claiborne A., Fahey R.C., Helmann J.D.;
RT "Biosynthesis and functions of bacillithiol, a major low-molecular-weight
RT thiol in Bacilli.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:6482-6486(2010).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (1.77 ANGSTROMS) IN COMPLEX WITH ADP, AND SUBUNIT.
RC STRAIN=168;
RX PubMed=25496067; DOI=10.1021/bi501394q;
RA VanDuinen A.J., Winchell K.R., Keithly M.E., Cook P.D.;
RT "X-ray crystallographic structure of BshC, a unique enzyme involved in
RT bacillithiol biosynthesis.";
RL Biochemistry 54:100-103(2015).
CC -!- FUNCTION: Involved in bacillithiol (BSH) biosynthesis. May catalyze the
CC last step of the pathway, the addition of cysteine to glucosamine
CC malate (GlcN-Mal) to generate BSH. {ECO:0000255|HAMAP-Rule:MF_01867,
CC ECO:0000305|PubMed:20308541}.
CC -!- SUBUNIT: Homodimer in solution. {ECO:0000269|PubMed:25496067}.
CC -!- DISRUPTION PHENOTYPE: Mutant accumulates GlcN-Mal and does not produce
CC BSH. {ECO:0000269|PubMed:20308541}.
CC -!- SIMILARITY: Belongs to the BshC family. {ECO:0000255|HAMAP-
CC Rule:MF_01867, ECO:0000305}.
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DR EMBL; Z68230; CAA92523.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB13385.2; -; Genomic_DNA.
DR EMBL; Z98682; CAB11365.1; -; Genomic_DNA.
DR PIR; G69875; G69875.
DR RefSeq; NP_389395.2; NC_000964.3.
DR RefSeq; WP_003245571.1; NZ_JNCM01000035.1.
DR PDB; 4WBD; X-ray; 1.77 A; A=1-539.
DR PDBsum; 4WBD; -.
DR AlphaFoldDB; P55342; -.
DR SMR; P55342; -.
DR IntAct; P55342; 1.
DR STRING; 224308.BSU15120; -.
DR PaxDb; P55342; -.
DR PRIDE; P55342; -.
DR EnsemblBacteria; CAB13385; CAB13385; BSU_15120.
DR GeneID; 939844; -.
DR KEGG; bsu:BSU15120; -.
DR PATRIC; fig|224308.179.peg.1648; -.
DR eggNOG; COG4365; Bacteria.
DR OMA; TTGHQLN; -.
DR PhylomeDB; P55342; -.
DR BioCyc; BSUB:BSU15120-MON; -.
DR BioCyc; MetaCyc:BSU15120-MON; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-UniRule.
DR HAMAP; MF_01867; BshC; 1.
DR InterPro; IPR011199; Bacillithiol_biosynth_BshC.
DR Pfam; PF10079; BshC; 1.
DR PIRSF; PIRSF012535; UCP012535; 1.
DR TIGRFAMs; TIGR03998; thiol_BshC; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Coiled coil; Ligase; Reference proteome.
FT CHAIN 1..539
FT /note="Putative cysteine ligase BshC"
FT /id="PRO_0000049626"
FT COILED 455..475
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01867"
FT BINDING 146
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0000269|PubMed:25496067,
FT ECO:0007744|PDB:4WBD"
FT BINDING 384..386
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0000269|PubMed:25496067,
FT ECO:0007744|PDB:4WBD"
FT BINDING 490..493
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0000269|PubMed:25496067,
FT ECO:0007744|PDB:4WBD"
FT BINDING 506
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0000269|PubMed:25496067,
FT ECO:0007744|PDB:4WBD"
FT BINDING 510
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0000269|PubMed:25496067,
FT ECO:0007744|PDB:4WBD"
FT CONFLICT 63
FT /note="Y -> S (in Ref. 1; CAA92523)"
FT /evidence="ECO:0000305"
FT CONFLICT 69
FT /note="S -> P (in Ref. 1; CAA92523)"
FT /evidence="ECO:0000305"
FT CONFLICT 74
FT /note="S -> T (in Ref. 1; CAA92523)"
FT /evidence="ECO:0000305"
FT CONFLICT 78..84
FT /note="KLKDPSS -> TLKTRHV (in Ref. 1; CAA92523)"
FT /evidence="ECO:0000305"
FT CONFLICT 415
FT /note="E -> A (in Ref. 1; CAA92523)"
FT /evidence="ECO:0000305"
FT STRAND 2..6
FT /evidence="ECO:0007829|PDB:4WBD"
FT HELIX 13..20
FT /evidence="ECO:0007829|PDB:4WBD"
FT HELIX 23..27
FT /evidence="ECO:0007829|PDB:4WBD"
FT HELIX 38..47
FT /evidence="ECO:0007829|PDB:4WBD"
FT HELIX 53..64
FT /evidence="ECO:0007829|PDB:4WBD"
FT HELIX 65..67
FT /evidence="ECO:0007829|PDB:4WBD"
FT HELIX 70..78
FT /evidence="ECO:0007829|PDB:4WBD"
FT STRAND 85..91
FT /evidence="ECO:0007829|PDB:4WBD"
FT HELIX 95..97
FT /evidence="ECO:0007829|PDB:4WBD"
FT HELIX 100..120
FT /evidence="ECO:0007829|PDB:4WBD"
FT STRAND 124..130
FT /evidence="ECO:0007829|PDB:4WBD"
FT HELIX 137..139
FT /evidence="ECO:0007829|PDB:4WBD"
FT STRAND 141..147
FT /evidence="ECO:0007829|PDB:4WBD"
FT STRAND 150..155
FT /evidence="ECO:0007829|PDB:4WBD"
FT TURN 166..168
FT /evidence="ECO:0007829|PDB:4WBD"
FT HELIX 173..185
FT /evidence="ECO:0007829|PDB:4WBD"
FT HELIX 193..205
FT /evidence="ECO:0007829|PDB:4WBD"
FT HELIX 210..222
FT /evidence="ECO:0007829|PDB:4WBD"
FT HELIX 223..225
FT /evidence="ECO:0007829|PDB:4WBD"
FT STRAND 228..231
FT /evidence="ECO:0007829|PDB:4WBD"
FT HELIX 235..250
FT /evidence="ECO:0007829|PDB:4WBD"
FT HELIX 252..268
FT /evidence="ECO:0007829|PDB:4WBD"
FT STRAND 281..288
FT /evidence="ECO:0007829|PDB:4WBD"
FT STRAND 291..298
FT /evidence="ECO:0007829|PDB:4WBD"
FT STRAND 301..304
FT /evidence="ECO:0007829|PDB:4WBD"
FT HELIX 305..307
FT /evidence="ECO:0007829|PDB:4WBD"
FT STRAND 309..311
FT /evidence="ECO:0007829|PDB:4WBD"
FT HELIX 313..322
FT /evidence="ECO:0007829|PDB:4WBD"
FT HELIX 324..326
FT /evidence="ECO:0007829|PDB:4WBD"
FT STRAND 327..329
FT /evidence="ECO:0007829|PDB:4WBD"
FT TURN 331..333
FT /evidence="ECO:0007829|PDB:4WBD"
FT HELIX 334..341
FT /evidence="ECO:0007829|PDB:4WBD"
FT STRAND 344..349
FT /evidence="ECO:0007829|PDB:4WBD"
FT HELIX 351..358
FT /evidence="ECO:0007829|PDB:4WBD"
FT HELIX 361..366
FT /evidence="ECO:0007829|PDB:4WBD"
FT STRAND 374..376
FT /evidence="ECO:0007829|PDB:4WBD"
FT STRAND 380..383
FT /evidence="ECO:0007829|PDB:4WBD"
FT HELIX 385..393
FT /evidence="ECO:0007829|PDB:4WBD"
FT HELIX 398..404
FT /evidence="ECO:0007829|PDB:4WBD"
FT HELIX 407..416
FT /evidence="ECO:0007829|PDB:4WBD"
FT HELIX 420..445
FT /evidence="ECO:0007829|PDB:4WBD"
FT HELIX 449..451
FT /evidence="ECO:0007829|PDB:4WBD"
FT HELIX 452..480
FT /evidence="ECO:0007829|PDB:4WBD"
FT HELIX 482..495
FT /evidence="ECO:0007829|PDB:4WBD"
FT HELIX 497..499
FT /evidence="ECO:0007829|PDB:4WBD"
FT HELIX 502..505
FT /evidence="ECO:0007829|PDB:4WBD"
FT HELIX 508..525
FT /evidence="ECO:0007829|PDB:4WBD"
FT STRAND 534..538
FT /evidence="ECO:0007829|PDB:4WBD"
SQ SEQUENCE 539 AA; 62668 MW; 86DBC2919B92E690 CRC64;
MQLTELSIKN QNVFVQHYID GKEEMSSFFD YSIHHKDMWR ERLEDLSSRF FAREELAAYL
TSYHNKFGSS AMQSAIEKLK DPSSAAVVGG QQAGLLTGPL YTIHKIISII VLAKQQEKEL
QVPVIPIFWV AGEDHDLDEI NFVHTSEENG PVKKKLPQSY WKKSSAASTS LDQEKCAAWI
DDVFAAFEET DHTNTLLDNV KRCLRESVTF TDFFELLIAD LFQEEGLVLL NSGDPGIKKL
ETAMFQKILR ENDELARAVS DQQAFMRQAG YKPIIESGKE QANLFYEYED ERFLIEKDNG
RFVIKELDLG WTRDELHTHM EEHPERFSNN VVTRPLMQEF LIPTLAFIAG PGEINYWGEL
KQAFAVMGFK MPPVMPRLNI TILERHIEKK LAERNISLQD AIERGTENQR ETYFERQIPE
EFTAVMDQAK SQIEAIHKTV RQEALKVDQS LEPLLLKNAA FIQDQLQFLE RTVMKRIEEK
EGYVLKDYER IQNSIKPLLA PQERIWNIMY YLNRYGPKFF TTFKNLPFSF QNQHQVVKL
