ID   HRP1_MYCTO              Reviewed;         143 AA.
AC   P9WJA2; L0TBT6; O06186; Q7D6V4;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   03-AUG-2022, entry version 32.
DE   RecName: Full=Hypoxic response protein 1;
DE            Short=HRP1;
GN   Name=hrp1; OrderedLocusNames=MT2701;
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).
RN   [2]
RP   INDUCTION BY NITRIC OXIDE (NO); BY HYPOXIA; IN MOUSE MODEL AND DORMANCY
RP   REGULON.
RC   STRAIN=CDC 1551 / Oshkosh;
RX   PubMed=12953092; DOI=10.1084/jem.20030205;
RA   Voskuil M.I., Schnappinger D., Visconti K.C., Harrell M.I., Dolganov G.M.,
RA   Sherman D.R., Schoolnik G.K.;
RT   "Inhibition of respiration by nitric oxide induces a Mycobacterium
RT   tuberculosis dormancy program.";
RL   J. Exp. Med. 198:705-713(2003).
CC   -!- FUNCTION: Unlike some other CBS-domain containing proteins does not
CC       seem to bind AMP. {ECO:0000250}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}. Note=Not seen to be
CC       associated with the cell wall. {ECO:0000250}.
CC   -!- INDUCTION: A member of the dormancy regulon. Induced in response to
CC       reduced oxygen tension (hypoxia) and low levels of nitric oxide (NO).
CC       {ECO:0000269|PubMed:12953092}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AE000516; AAK47017.1; -; Genomic_DNA.
DR   PIR; A70573; A70573.
DR   RefSeq; WP_003413598.1; NZ_KK341227.1.
DR   AlphaFoldDB; P9WJA2; -.
DR   SMR; P9WJA2; -.
DR   EnsemblBacteria; AAK47017; AAK47017; MT2701.
DR   GeneID; 45426630; -.
DR   KEGG; mtc:MT2701; -.
DR   PATRIC; fig|83331.31.peg.2912; -.
DR   HOGENOM; CLU_040681_12_0_11; -.
DR   Proteomes; UP000001020; Chromosome.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   Gene3D; 3.10.580.10; -; 1.
DR   InterPro; IPR000644; CBS_dom.
DR   InterPro; IPR046342; CBS_dom_sf.
DR   Pfam; PF00571; CBS; 2.
DR   SMART; SM00116; CBS; 2.
DR   SUPFAM; SSF54631; SSF54631; 1.
DR   PROSITE; PS51371; CBS; 2.
PE   2: Evidence at transcript level;
KW   CBS domain; Disulfide bond; Metal-binding; Repeat; Secreted; Zinc.
FT   CHAIN           1..143
FT                   /note="Hypoxic response protein 1"
FT                   /id="PRO_0000427865"
FT   DOMAIN          8..65
FT                   /note="CBS 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00703"
FT   DOMAIN          73..131
FT                   /note="CBS 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00703"
FT   BINDING         97
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         122
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   DISULFID        14..39
FT                   /evidence="ECO:0000250"
FT   DISULFID        136
FT                   /note="Interchain"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   143 AA;  15518 MW;  CF65AA9144341038 CRC64;
     MTTARDIMNA GVTCVGEHET LTAAAQYMRE HDIGALPICG DDDRLHGMLT DRDIVIKGLA
     AGLDPNTATA GELARDSIYY VDANASIQEM LNVMEEHQVR RVPVISEHRL VGIVTEADIA
     RHLPEHAIVQ FVKAICSPMA LAS