ID   TRHBO_MYCTO             Reviewed;         128 AA.
AC   P9WN22; L0TBB1; O53197; P0A595;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   03-AUG-2022, entry version 39.
DE   RecName: Full=Group 2 truncated hemoglobin GlbO;
DE   AltName: Full=Hemoglobin-like protein HbO;
DE   AltName: Full=Truncated hemoglobin;
DE            Short=trHbO;
GN   Name=glbO; OrderedLocusNames=MT2546;
OS   Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=83331;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CDC 1551 / Oshkosh;
RX   PubMed=12218036; DOI=10.1128/jb.184.19.5479-5490.2002;
RA   Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O.,
RA   Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K.,
RA   Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L.,
RA   Delcher A., Utterback T.R., Weidman J.F., Khouri H.M., Gill J., Mikula A.,
RA   Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M.;
RT   "Whole-genome comparison of Mycobacterium tuberculosis clinical and
RT   laboratory strains.";
RL   J. Bacteriol. 184:5479-5490(2002).
CC   -!- FUNCTION: When expressed in E.coli and M.smegmatis, HbO increases
CC       oxygen uptake. Membrane vesicles of E.coli carrying HbO show a
CC       respiration activity about twice that of membranes without HbO. HbO
CC       seems to interact with a terminal oxidase. Therefore, HbO could
CC       participate in oxygen/electron-transfer process, suggesting a function
CC       related to the facilitation of oxygen transfer during aerobic
CC       metabolism of M.tuberculosis (By similarity). {ECO:0000250}.
CC   -!- COFACTOR:
CC       Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250};
CC       Note=Binds 1 heme group per subunit. {ECO:0000250};
CC   -!- SUBUNIT: Homododecamer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Peripheral membrane
CC       protein {ECO:0000250}.
CC   -!- PTM: Contains L-DOPA (3',4'-dihydroxyphenylalanine). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the truncated hemoglobin family. Group II
CC       subfamily. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAK46846.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AE000516; AAK46846.1; ALT_INIT; Genomic_DNA.
DR   PIR; E70866; E70866.
DR   RefSeq; WP_003412688.1; NZ_KK341227.1.
DR   AlphaFoldDB; P9WN22; -.
DR   SMR; P9WN22; -.
DR   EnsemblBacteria; AAK46846; AAK46846; MT2546.
DR   GeneID; 45426463; -.
DR   KEGG; mtc:MT2546; -.
DR   PATRIC; fig|83331.31.peg.2747; -.
DR   HOGENOM; CLU_103526_3_1_11; -.
DR   Proteomes; UP000001020; Chromosome.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
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:0005344; F:oxygen carrier activity; IEA:UniProtKB-KW.
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   3: Inferred from homology;
KW   Cell membrane; Heme; Hydroxylation; Iron; Membrane; Metal-binding;
KW   Oxygen transport; Transport.
FT   CHAIN           1..128
FT                   /note="Group 2 truncated hemoglobin GlbO"
FT                   /id="PRO_0000427202"
FT   BINDING         75
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                   /evidence="ECO:0000250"
FT   MOD_RES         36
FT                   /note="3',4'-dihydroxyphenylalanine"
FT                   /evidence="ECO:0000250"
FT   CROSSLNK        23..36
FT                   /note="Isodityrosine (Tyr-Tyr)"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   128 AA;  14950 MW;  CEF4CD23907B0CCA CRC64;
     MPKSFYDAVG GAKTFDAIVS RFYAQVAEDE VLRRVYPEDD LAGAEERLRM FLEQYWGGPR
     TYSEQRGHPR LRMRHAPFRI SLIERDAWLR CMHTAVASID SETLDDEHRR ELLDYLEMAA
     HSLVNSPF