DIPZ_MYCTO
ID DIPZ_MYCTO Reviewed; 695 AA.
AC P9WG62; L0TB47; Q10801;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 25-MAY-2022, entry version 36.
DE RecName: Full=Protein DipZ;
GN Name=dipZ; OrderedLocusNames=MT2942;
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 -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
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DR EMBL; AE000516; AAK47267.1; -; Genomic_DNA.
DR PIR; E70923; E70923.
DR RefSeq; WP_003414635.1; NZ_KK341227.1.
DR AlphaFoldDB; P9WG62; -.
DR SMR; P9WG62; -.
DR EnsemblBacteria; AAK47267; AAK47267; MT2942.
DR KEGG; mtc:MT2942; -.
DR PATRIC; fig|83331.31.peg.3179; -.
DR HOGENOM; CLU_033708_0_0_11; -.
DR Proteomes; UP000001020; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016209; F:antioxidant activity; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR GO; GO:0017004; P:cytochrome complex assembly; IEA:InterPro.
DR InterPro; IPR000866; AhpC/TSA.
DR InterPro; IPR003834; Cyt_c_assmbl_TM_dom.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR041017; Thioredoxin_10.
DR InterPro; IPR013766; Thioredoxin_domain.
DR Pfam; PF00578; AhpC-TSA; 1.
DR Pfam; PF02683; DsbD; 1.
DR Pfam; PF17991; Thioredoxin_10; 1.
DR SUPFAM; SSF52833; SSF52833; 1.
DR PROSITE; PS51352; THIOREDOXIN_2; 1.
PE 4: Predicted;
KW Cell membrane; Membrane; Transmembrane; Transmembrane helix.
FT CHAIN 1..695
FT /note="Protein DipZ"
FT /id="PRO_0000428417"
FT TRANSMEM 123..143
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 179..199
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 205..225
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 254..274
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 285..305
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 325..345
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 394..542
FT /note="Thioredoxin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
SQ SEQUENCE 695 AA; 74120 MW; 16B8ADEE33FF73DA CRC64;
MVESRRAAAA ASAYASRCGI APATSQRSLA TPPTISVPSG EGRCRCHVAR GAGRDPRRRL
RRRRWCGRCG YHSHLTGGEF DVNRLCQQRS RERSCQLVAV PADPRPKRQR ITDVLTLALV
GFLGGLITGI SPCILPVLPV IFFSGAQSVD AAQVAKPEGA VAVRRKRALS ATLRPYRVIG
GLVLSFGMVT LLGSALLSVL HLPQDAIRWA ALVALVAIGA GLIFPRFEQL LEKPFSRIPQ
KQIVTRSNGF GLGLALGVLY VPCAGPILAA IVVAGATATI GLGTVVLTAT FALGAALPLL
FFALAGQRIA ERVGAFRRRQ REIRIATGSV TILLAVALVF DLPAALQRAI PDYTASLQQQ
ISTGTEIREQ LNLGGIVNAQ NAQLSNCSDG AAQLESCGTA PDLKGITGWL NTPGNKPIDL
KSLRGKVVLI DFWAYSCINC QRAIPHVVGW YQAYKDSGLA VIGVHTPEYA FEKVPGNVAK
GAANLGISYP IALDNNYATW TNYRNRYWPA EYLIDATGTV RHIKFGEGDY NVTETLVRQL
LNDAKPGVKL PQPSSTTTPD LTPRAALTPE TYFGVGKVVN YGGGGAYDEG SAVFDYPPSL
AANSFALRGR WALDYQGATS DGNDAAIKLN YHAKDVYIVV GGTGTLTVVR DGKPATLPIS
GPPTTHQVVA GDRLASETLE VRPSKGLQVF SFTYG