DIPZ_MYCTU
ID DIPZ_MYCTU Reviewed; 695 AA.
AC P9WG63; L0TB47; Q10801;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 25-MAY-2022, entry version 37.
DE RecName: Full=Protein DipZ;
GN Name=dipZ; OrderedLocusNames=Rv2874; ORFNames=MTCY274.05;
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 [GENOMIC DNA].
RC STRAIN=ATCC 25618 / H37Rv;
RA Juarez M.D., Torres A., Bigi F., Espitia C.;
RT "Mycobacterium tuberculosis mpt83 and dipZ/thioredoxin genes are part of
RT the same translational unit.";
RL Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases.
RN [2]
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).
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
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DR EMBL; AF189006; AAF13401.1; -; Genomic_DNA.
DR EMBL; AL123456; CCP45676.1; -; Genomic_DNA.
DR PIR; E70923; E70923.
DR RefSeq; NP_217390.1; NC_000962.3.
DR RefSeq; WP_009936521.1; NC_000962.3.
DR PDB; 2HYX; X-ray; 1.90 A; A/B/C/D=366-695.
DR PDB; 5CYY; X-ray; 2.20 A; A/B/C/D=361-695.
DR PDBsum; 2HYX; -.
DR PDBsum; 5CYY; -.
DR AlphaFoldDB; P9WG63; -.
DR SMR; P9WG63; -.
DR STRING; 83332.Rv2874; -.
DR TCDB; 5.A.1.2.9; the disulfide bond oxidoreductase d (dsbd) family.
DR PaxDb; P9WG63; -.
DR DNASU; 888162; -.
DR GeneID; 888162; -.
DR KEGG; mtu:Rv2874; -.
DR TubercuList; Rv2874; -.
DR eggNOG; COG0526; Bacteria.
DR eggNOG; COG0785; Bacteria.
DR OMA; GQIRYHH; -.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; HDA:MTBBASE.
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 1: Evidence at protein level;
KW 3D-structure; Cell membrane; Membrane; Reference proteome; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..695
FT /note="Protein DipZ"
FT /id="PRO_0000079911"
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"
FT TURN 379..383
FT /evidence="ECO:0007829|PDB:2HYX"
FT HELIX 384..386
FT /evidence="ECO:0007829|PDB:2HYX"
FT STRAND 408..412
FT /evidence="ECO:0007829|PDB:2HYX"
FT HELIX 413..415
FT /evidence="ECO:0007829|PDB:2HYX"
FT HELIX 420..423
FT /evidence="ECO:0007829|PDB:2HYX"
FT STRAND 426..433
FT /evidence="ECO:0007829|PDB:2HYX"
FT HELIX 438..454
FT /evidence="ECO:0007829|PDB:2HYX"
FT HELIX 455..457
FT /evidence="ECO:0007829|PDB:2HYX"
FT STRAND 459..465
FT /evidence="ECO:0007829|PDB:2HYX"
FT HELIX 470..473
FT /evidence="ECO:0007829|PDB:2HYX"
FT HELIX 475..485
FT /evidence="ECO:0007829|PDB:2HYX"
FT STRAND 491..493
FT /evidence="ECO:0007829|PDB:2HYX"
FT HELIX 498..502
FT /evidence="ECO:0007829|PDB:2HYX"
FT STRAND 507..514
FT /evidence="ECO:0007829|PDB:2HYX"
FT STRAND 518..527
FT /evidence="ECO:0007829|PDB:2HYX"
FT HELIX 530..544
FT /evidence="ECO:0007829|PDB:2HYX"
FT HELIX 554..556
FT /evidence="ECO:0007829|PDB:2HYX"
FT TURN 575..577
FT /evidence="ECO:0007829|PDB:2HYX"
FT STRAND 589..594
FT /evidence="ECO:0007829|PDB:2HYX"
FT STRAND 604..613
FT /evidence="ECO:0007829|PDB:2HYX"
FT STRAND 618..620
FT /evidence="ECO:0007829|PDB:2HYX"
FT STRAND 622..624
FT /evidence="ECO:0007829|PDB:2HYX"
FT STRAND 626..650
FT /evidence="ECO:0007829|PDB:2HYX"
FT STRAND 653..659
FT /evidence="ECO:0007829|PDB:2HYX"
FT STRAND 664..683
FT /evidence="ECO:0007829|PDB:2HYX"
FT STRAND 688..695
FT /evidence="ECO:0007829|PDB:2HYX"
SQ SEQUENCE 695 AA; 74168 MW; B775ADEE33FF73CF 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 GYRLASETLE VRPSKGLQVF SFTYG
