TRHBO_BACSU
ID TRHBO_BACSU Reviewed; 132 AA.
AC O31607;
DT 13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Group 2 truncated hemoglobin YjbI;
DE Short=Truncated Hb;
DE Short=trHbO;
DE AltName: Full=Hemoglobin-like protein YjbI;
DE AltName: Full=Truncated BHb;
GN Name=yjbI; OrderedLocusNames=BSU11560;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
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 [2]
RP CHARACTERIZATION AS A HEME PROTEIN, FUNCTION AS A PEROXIDASE, AND SUBUNIT.
RX PubMed=15866723; DOI=10.1016/j.pep.2005.02.022;
RA Choudhary M.L., Jawaid S., Ahuja M.K., Shiva N.K., Gupta P., Bhuyan A.K.,
RA Khatri G.S.;
RT "Open reading frame yjbI of Bacillus subtilis codes for truncated
RT hemoglobin.";
RL Protein Expr. Purif. 41:363-372(2005).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS) OF COMPLEX WITH HEME.
RX PubMed=15590662; DOI=10.1074/jbc.m407267200;
RA Giangiacomo L., Ilari A., Boffi A., Morea V., Chiancone E.;
RT "The truncated oxygen-avid hemoglobin from Bacillus subtilis: X-ray
RT structure and ligand binding properties.";
RL J. Biol. Chem. 280:9192-9202(2005).
CC -!- FUNCTION: Hemoglobin-like protein that exhibits a low peroxidase
CC activity. Its very high oxygen affinity may rule out the possibility
CC that it is involved in oxygen transport. {ECO:0000269|PubMed:15866723}.
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Note=Binds 1 heme group per subunit.;
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:15866723}.
CC -!- SIMILARITY: Belongs to the truncated hemoglobin family. Group II
CC subfamily. {ECO:0000305}.
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DR EMBL; AL009126; CAB13013.1; -; Genomic_DNA.
DR PIR; A69844; A69844.
DR RefSeq; NP_389038.1; NC_000964.3.
DR RefSeq; WP_003232928.1; NZ_JNCM01000035.1.
DR PDB; 1UX8; X-ray; 2.15 A; A=1-132.
DR PDBsum; 1UX8; -.
DR AlphaFoldDB; O31607; -.
DR SMR; O31607; -.
DR STRING; 224308.BSU11560; -.
DR PaxDb; O31607; -.
DR PRIDE; O31607; -.
DR EnsemblBacteria; CAB13013; CAB13013; BSU_11560.
DR GeneID; 936416; -.
DR KEGG; bsu:BSU11560; -.
DR PATRIC; fig|224308.179.peg.1245; -.
DR eggNOG; COG2346; Bacteria.
DR InParanoid; O31607; -.
DR OMA; QYWGGPT; -.
DR PhylomeDB; O31607; -.
DR BioCyc; BSUB:BSU11560-MON; -.
DR EvolutionaryTrace; O31607; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0019825; F:oxygen binding; IEA:InterPro.
DR GO; GO:0008379; F:thioredoxin peroxidase activity; IBA:GO_Central.
DR GO; GO:0045454; P:cell redox homeostasis; IBA:GO_Central.
DR GO; GO:0034599; P:cellular response to oxidative stress; IBA:GO_Central.
DR GO; GO:0015671; P:oxygen transport; IEA:InterPro.
DR Gene3D; 1.10.490.10; -; 1.
DR InterPro; IPR009050; Globin-like_sf.
DR InterPro; IPR012292; Globin/Proto.
DR InterPro; IPR019795; Globin_bac-like_CS.
DR InterPro; IPR001486; Hemoglobin_trunc.
DR Pfam; PF01152; Bac_globin; 1.
DR SUPFAM; SSF46458; SSF46458; 1.
DR PROSITE; PS01213; GLOBIN_FAM_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Heme; Iron; Metal-binding; Reference proteome; Transport.
FT CHAIN 1..132
FT /note="Group 2 truncated hemoglobin YjbI"
FT /id="PRO_0000162647"
FT BINDING 45
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT BINDING 48
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT BINDING 63
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT BINDING 76
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="proximal binding residue"
FT HELIX 8..11
FT /evidence="ECO:0007829|PDB:1UX8"
FT HELIX 13..30
FT /evidence="ECO:0007829|PDB:1UX8"
FT TURN 32..34
FT /evidence="ECO:0007829|PDB:1UX8"
FT HELIX 35..37
FT /evidence="ECO:0007829|PDB:1UX8"
FT HELIX 43..56
FT /evidence="ECO:0007829|PDB:1UX8"
FT HELIX 62..67
FT /evidence="ECO:0007829|PDB:1UX8"
FT HELIX 72..76
FT /evidence="ECO:0007829|PDB:1UX8"
FT HELIX 83..100
FT /evidence="ECO:0007829|PDB:1UX8"
FT HELIX 105..121
FT /evidence="ECO:0007829|PDB:1UX8"
SQ SEQUENCE 132 AA; 15116 MW; 61B970CF4CCD52A1 CRC64;
MGQSFNAPYE AIGEELLSQL VDTFYERVAS HPLLKPIFPS DLTETARKQK QFLTQYLGGP
PLYTEEHGHP MLRARHLPFP ITNERADAWL SCMKDAMDHV GLEGEIREFL FGRLELTARH
MVNQTEAEDR SS
