ID   Y2850_MYCTO             Reviewed;         629 AA.
AC   P9WPR2; L0TB22; O05809;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   25-MAY-2022, entry version 32.
DE   RecName: Full=Uncharacterized protein MT2916;
GN   OrderedLocusNames=MT2916;
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   -!- SIMILARITY: Belongs to the Mg-chelatase subunits D/I family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAK47242.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; AE000516; AAK47242.1; ALT_FRAME; Genomic_DNA.
DR   PIR; E70589; E70589.
DR   AlphaFoldDB; P9WPR2; -.
DR   SMR; P9WPR2; -.
DR   EnsemblBacteria; AAK47242; AAK47242; MT2916.
DR   KEGG; mtc:MT2916; -.
DR   HOGENOM; CLU_016684_6_0_11; -.
DR   Proteomes; UP000001020; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   CDD; cd01451; vWA_Magnesium_chelatase; 1.
DR   Gene3D; 3.40.50.300; -; 1.
DR   Gene3D; 3.40.50.410; -; 1.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR011704; ATPase_dyneun-rel_AAA.
DR   InterPro; IPR041702; BchD/ChlD_VWA.
DR   InterPro; IPR041628; ChlI/MoxR_AAA_lid.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR002035; VWF_A.
DR   InterPro; IPR036465; vWFA_dom_sf.
DR   Pfam; PF07728; AAA_5; 1.
DR   Pfam; PF17863; AAA_lid_2; 1.
DR   Pfam; PF13519; VWA_2; 1.
DR   SMART; SM00382; AAA; 1.
DR   SMART; SM00327; VWA; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   SUPFAM; SSF53300; SSF53300; 1.
DR   PROSITE; PS50234; VWFA; 1.
PE   3: Inferred from homology;
FT   CHAIN           1..629
FT                   /note="Uncharacterized protein MT2916"
FT                   /id="PRO_0000426907"
FT   DOMAIN          451..587
FT                   /note="VWFA"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00219"
FT   REGION          308..395
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        322..341
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        345..362
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   629 AA;  66987 MW;  F4ACB04E3E5B526F CRC64;
     MKPYPFSAIV GHDRLRLALL LCAVRPEIGG ALIRGEKGTA KSTAVRGLAA LLSVATGSTE
     TGLVELPLGA TEDRVVGSLD LQRVMRDGEH AFSPGLLARA HGGVLYVDEV NLLHDHLVDI
     LLDAAAMGRV HVERDGISHS HEARFVLIGT MNPEEGELRP QLLDRFGLTV DVQASRDIDV
     RVQVIRRRMA YEADPDAFVA RYADADAELA HRIAAARATV DDVVLGDNEL RRIAALCAAF
     DVDGMRADLV VARTAAAHAA WRGVRTVEEQ DIRAAAELAL PHRRRRDPFD DHGIDRDQLD
     EALALASVDP EPEPDPPGGG QSANEPASQP NSRSKSTEPG APSSMGDDPP RPASPRLRSS
     PRPSAPPSKI FRTRALRVPG VGTGAPGRRS RARNASGSVV AAAEVSDPDA HGLHLFATLL
     AAGERAFGAG PLRPWPDDVR RAIREGREGN LVIFVVDASG SMAARDRMAA VSGATLSLLR
     DAYQRRDKVA VITFRQHEAT LLLSPTSSAH IAGRRLARFS TGGKTPLAEG LLAARALIIR
     EKVRDRARRP LVVVLTDGRA TAGPDPLGRS RTAAAGLVAE GAAAVVVDCE TSYVRLGLAA
     QLARQLGAPV VRLEQLHADY LVHAVRGVA