TRHBO_MYCTU
ID TRHBO_MYCTU Reviewed; 128 AA.
AC P9WN23; 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 40.
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=Rv2470; ORFNames=MTV008.26;
OS Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83332;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=9634230; DOI=10.1038/31159;
RA Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA Barrell B.G.;
RT "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT genome sequence.";
RL Nature 393:537-544(1998).
RN [2]
RP CHARACTERIZATION.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=11796724; DOI=10.1074/jbc.m111478200;
RA Pathania R., Navani N.K., Rajamohan G., Dikshit K.L.;
RT "Mycobacterium tuberculosis hemoglobin HbO associates with membranes and
RT stimulates cellular respiration of recombinant Escherichia coli.";
RL J. Biol. Chem. 277:15293-15302(2002).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=21969609; DOI=10.1074/mcp.m111.011627;
RA Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K.,
RA Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R.,
RA Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M.,
RA Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.;
RT "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution
RT mass spectrometry.";
RL Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.11 ANGSTROMS), AND HYDROXYLATION AT TYR-36.
RX PubMed=12719529; DOI=10.1073/pnas.1037676100;
RA Milani M., Savard P.-Y., Ouellet H., Ascenzi P., Guertin M., Bolognesi M.;
RT "A TyrCD1/TrpG8 hydrogen bond network and a TyrB10TyrCD1 covalent link
RT shape the heme distal site of Mycobacterium tuberculosis hemoglobin O.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:5766-5771(2003).
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.
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Note=Binds 1 heme group per subunit.;
CC -!- SUBUNIT: Homododecamer.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Peripheral membrane
CC protein {ECO:0000305}.
CC -!- PTM: Contains L-DOPA (3',4'-dihydroxyphenylalanine).
CC -!- SIMILARITY: Belongs to the truncated hemoglobin family. Group II
CC subfamily. {ECO:0000305}.
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DR EMBL; AL123456; CCP45264.1; -; Genomic_DNA.
DR PIR; E70866; E70866.
DR RefSeq; NP_216986.1; NC_000962.3.
DR RefSeq; WP_003412688.1; NZ_NVQJ01000024.1.
DR PDB; 1NGK; X-ray; 2.11 A; A/B/C/D/E/F/G/H/I/J/K/L=1-128.
DR PDB; 2QRW; X-ray; 1.93 A; A/B/C/D/E/F/G/H/I/J/K/L=1-128.
DR PDBsum; 1NGK; -.
DR PDBsum; 2QRW; -.
DR AlphaFoldDB; P9WN23; -.
DR SMR; P9WN23; -.
DR DIP; DIP-16963N; -.
DR STRING; 83332.Rv2470; -.
DR PaxDb; P9WN23; -.
DR DNASU; 887743; -.
DR GeneID; 45426463; -.
DR GeneID; 887743; -.
DR KEGG; mtu:Rv2470; -.
DR TubercuList; Rv2470; -.
DR eggNOG; COG2346; Bacteria.
DR OMA; QYWGGPT; -.
DR PhylomeDB; P9WN23; -.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IDA:MTBBASE.
DR GO; GO:0020037; F:heme binding; IDA:MTBBASE.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0019825; F:oxygen binding; IDA:MTBBASE.
DR GO; GO:0005344; F:oxygen carrier activity; IEA:UniProtKB-KW.
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; IDA:MTBBASE.
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; Cell membrane; Heme; Hydroxylation; Iron; Membrane;
KW Metal-binding; Oxygen transport; Reference proteome; Transport.
FT CHAIN 1..128
FT /note="Group 2 truncated hemoglobin GlbO"
FT /id="PRO_0000162643"
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 MOD_RES 36
FT /note="3',4'-dihydroxyphenylalanine; alternate"
FT /evidence="ECO:0000269|PubMed:12719529"
FT CROSSLNK 23..36
FT /note="Isodityrosine (Tyr-Tyr); alternate"
FT HELIX 5..8
FT /evidence="ECO:0007829|PDB:2QRW"
FT TURN 9..11
FT /evidence="ECO:0007829|PDB:2QRW"
FT HELIX 12..28
FT /evidence="ECO:0007829|PDB:2QRW"
FT HELIX 30..35
FT /evidence="ECO:0007829|PDB:2QRW"
FT HELIX 42..55
FT /evidence="ECO:0007829|PDB:2QRW"
FT HELIX 61..66
FT /evidence="ECO:0007829|PDB:2QRW"
FT HELIX 71..75
FT /evidence="ECO:0007829|PDB:2QRW"
FT HELIX 82..97
FT /evidence="ECO:0007829|PDB:2QRW"
FT TURN 101..103
FT /evidence="ECO:0007829|PDB:2QRW"
FT HELIX 106..122
FT /evidence="ECO:0007829|PDB:2QRW"
SQ SEQUENCE 128 AA; 14950 MW; CEF4CD23907B0CCA CRC64;
MPKSFYDAVG GAKTFDAIVS RFYAQVAEDE VLRRVYPEDD LAGAEERLRM FLEQYWGGPR
TYSEQRGHPR LRMRHAPFRI SLIERDAWLR CMHTAVASID SETLDDEHRR ELLDYLEMAA
HSLVNSPF
