TRHBP_CAMJE
ID TRHBP_CAMJE Reviewed; 127 AA.
AC Q0PB48;
DT 20-APR-2010, integrated into UniProtKB/Swiss-Prot.
DT 19-SEP-2006, sequence version 1.
DT 03-AUG-2022, entry version 78.
DE RecName: Full=Group 3 truncated hemoglobin ctb;
DE Short=Cj-trHbP;
DE Short=Truncated Hb;
GN Name=ctb; OrderedLocusNames=Cj0465c;
OS Campylobacter jejuni subsp. jejuni serotype O:2 (strain ATCC 700819 / NCTC
OS 11168).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Campylobacteraceae; Campylobacter.
OX NCBI_TaxID=192222;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700819 / NCTC 11168;
RX PubMed=10688204; DOI=10.1038/35001088;
RA Parkhill J., Wren B.W., Mungall K.L., Ketley J.M., Churcher C.M.,
RA Basham D., Chillingworth T., Davies R.M., Feltwell T., Holroyd S.,
RA Jagels K., Karlyshev A.V., Moule S., Pallen M.J., Penn C.W., Quail M.A.,
RA Rajandream M.A., Rutherford K.M., van Vliet A.H.M., Whitehead S.,
RA Barrell B.G.;
RT "The genome sequence of the food-borne pathogen Campylobacter jejuni
RT reveals hypervariable sequences.";
RL Nature 403:665-668(2000).
RN [2]
RP POSSIBLE FUNCTION, SUBCELLULAR LOCATION, INDUCTION, AND DISRUPTION
RP PHENOTYPE.
RC STRAIN=ATCC 700819 / NCTC 11168;
RX PubMed=16339953; DOI=10.1099/mic.0.28266-0;
RA Wainwright L.M., Elvers K.T., Park S.F., Poole R.K.;
RT "A truncated haemoglobin implicated in oxygen metabolism by the
RT microaerophilic food-borne pathogen Campylobacter jejuni.";
RL Microbiology 151:4079-4091(2005).
RN [3]
RP CHARACTERIZATION, HEME COFACTOR, AND SUBUNIT.
RC STRAIN=ATCC 700819 / NCTC 11168;
RX PubMed=16681372; DOI=10.1021/bi052247k;
RA Wainwright L.M., Wang Y., Park S.F., Yeh S.R., Poole R.K.;
RT "Purification and spectroscopic characterization of Ctb, a group III
RT truncated hemoglobin implicated in oxygen metabolism in the food-borne
RT pathogen Campylobacter jejuni.";
RL Biochemistry 45:6003-6011(2006).
RN [4]
RP POSSIBLE FUNCTION IN O(2) CHEMISTRY, AND MUTAGENESIS OF TYR-19 AND HIS-46.
RC STRAIN=ATCC 700819 / NCTC 11168;
RX PubMed=17339325; DOI=10.1074/jbc.m609397200;
RA Lu C., Egawa T., Wainwright L.M., Poole R.K., Yeh S.R.;
RT "Structural and functional properties of a truncated hemoglobin from a
RT food-borne pathogen Campylobacter jejuni.";
RL J. Biol. Chem. 282:13627-13636(2007).
RN [5]
RP POSSIBLE FUNCTION IN CYANIDE DETOXIFICATION.
RC STRAIN=ATCC 700819 / NCTC 11168;
RX PubMed=18190529; DOI=10.1111/j.1742-4658.2007.06223.x;
RA Bolli A., Ciaccio C., Coletta M., Nardini M., Bolognesi M., Pesce A.,
RA Guertin M., Visca P., Ascenzi P.;
RT "Ferrous Campylobacter jejuni truncated hemoglobin P displays an extremely
RT high reactivity for cyanide - a comparative study.";
RL FEBS J. 275:633-645(2008).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS) OF THE CYANO-MET FORM, HEME
RP COFACTOR, AND SUBUNIT.
RC STRAIN=ATCC 700819 / NCTC 11168;
RX PubMed=17023416; DOI=10.1074/jbc.m607254200;
RA Nardini M., Pesce A., Labarre M., Richard C., Bolli A., Ascenzi P.,
RA Guertin M., Bolognesi M.;
RT "Structural determinants in the group III truncated hemoglobin from
RT Campylobacter jejuni.";
RL J. Biol. Chem. 281:37803-37812(2006).
CC -!- FUNCTION: Has been suggested to be involved in cytochrome c peroxidase
CC or P450-like oxygen chemistry or cyanide detoxification. The high
CC oxygen affinity of this protein suggests that it probably does not
CC function as an oxygen transporter.
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Note=Binds 1 heme group per subunit; upon expression in E.coli it
CC purifies predominantly in the Fe(2+)-oxy form, binding O(2) tightly
CC even under anaerobic conditions.;
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:16681372,
CC ECO:0000269|PubMed:17023416}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305|PubMed:16339953}.
CC -!- INDUCTION: Constitutively expressed, it is further induced by S-
CC nitrosoglutathione (GSNO) and S-nitroso-N-acetylpenicillamine (SNAP)
CC (at protein level). {ECO:0000269|PubMed:16339953}.
CC -!- DISRUPTION PHENOTYPE: Cells lacking this gene grow less well than wild-
CC type under conditions of high aeration. {ECO:0000269|PubMed:16339953}.
CC -!- SIMILARITY: Belongs to the truncated hemoglobin family. Group III
CC subfamily. {ECO:0000305}.
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DR EMBL; AL111168; CAL34613.1; -; Genomic_DNA.
DR PIR; D81391; D81391.
DR RefSeq; WP_002858471.1; NC_002163.1.
DR RefSeq; YP_002343899.1; NC_002163.1.
DR PDB; 2IG3; X-ray; 2.15 A; A/B=1-127.
DR PDBsum; 2IG3; -.
DR AlphaFoldDB; Q0PB48; -.
DR SMR; Q0PB48; -.
DR IntAct; Q0PB48; 54.
DR STRING; 192222.Cj0465c; -.
DR PaxDb; Q0PB48; -.
DR EnsemblBacteria; CAL34613; CAL34613; Cj0465c.
DR GeneID; 904788; -.
DR KEGG; cje:Cj0465c; -.
DR PATRIC; fig|192222.6.peg.457; -.
DR eggNOG; COG2346; Bacteria.
DR HOGENOM; CLU_104957_4_0_7; -.
DR OMA; KLMDIFY; -.
DR EvolutionaryTrace; Q0PB48; -.
DR Proteomes; UP000000799; Chromosome.
DR GO; GO:0005737; C:cytoplasm; 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 Gene3D; 1.10.490.10; -; 1.
DR InterPro; IPR009050; Globin-like_sf.
DR InterPro; IPR012292; Globin/Proto.
DR InterPro; IPR001486; Hemoglobin_trunc.
DR Pfam; PF01152; Bac_globin; 1.
DR SUPFAM; SSF46458; SSF46458; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Heme; Iron; Metal-binding; Reference proteome;
KW Transport.
FT CHAIN 1..127
FT /note="Group 3 truncated hemoglobin ctb"
FT /id="PRO_0000393468"
FT BINDING 64
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT BINDING 72
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 MUTAGEN 19
FT /note="Y->F: Known as B10, reduces accessible space in the
FT distal pocket, retarding ligand binding. Enlarges distal
FT pocket, facilitating ligand entry; when associated with L-
FT 46."
FT /evidence="ECO:0000269|PubMed:17339325"
FT MUTAGEN 46
FT /note="H->L: Known as E7, reduces accessible space in the
FT distal pocket, retarding ligand binding. Enlarges distal
FT pocket, facilitating ligand entry; when associated with F-
FT 19."
FT /evidence="ECO:0000269|PubMed:17339325"
FT STRAND 3..5
FT /evidence="ECO:0007829|PDB:2IG3"
FT HELIX 8..24
FT /evidence="ECO:0007829|PDB:2IG3"
FT HELIX 28..36
FT /evidence="ECO:0007829|PDB:2IG3"
FT HELIX 40..58
FT /evidence="ECO:0007829|PDB:2IG3"
FT HELIX 68..73
FT /evidence="ECO:0007829|PDB:2IG3"
FT HELIX 82..97
FT /evidence="ECO:0007829|PDB:2IG3"
FT HELIX 100..121
FT /evidence="ECO:0007829|PDB:2IG3"
SQ SEQUENCE 127 AA; 14973 MW; BCFA4E43C4C9752C CRC64;
MKFETINQES IAKLMEIFYE KVRKDKDLGP IFNNAIGTSD EEWKEHKAKI GNFWAGMLLG
EGDYNGQPLK KHLDLPPFPQ EFFEIWLKLF EESLNIVYNE EMKNVILQRA QMIASHFQNM
LYKYGGH
