ID   Y1333_MYCTO             Reviewed;         344 AA.
AC   P9WM22; L0T6C1; P64811; Q10644;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   03-AUG-2022, entry version 33.
DE   RecName: Full=Uncharacterized aminopeptidase MT1375;
DE            EC=3.4.11.- {ECO:0000250|UniProtKB:Q52VH2};
GN   OrderedLocusNames=MT1375;
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   -!- FUNCTION: Aminopeptidase. {ECO:0000250|UniProtKB:Q52VH2}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC       protein {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the peptidase S58 family. {ECO:0000305}.
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DR   EMBL; AE000516; AAK45639.1; -; Genomic_DNA.
DR   PIR; A70771; A70771.
DR   RefSeq; WP_003406908.1; NZ_KK341227.1.
DR   AlphaFoldDB; P9WM22; -.
DR   SMR; P9WM22; -.
DR   MEROPS; P01.101; -.
DR   EnsemblBacteria; AAK45639; AAK45639; MT1375.
DR   KEGG; mtc:MT1375; -.
DR   PATRIC; fig|83331.31.peg.1482; -.
DR   HOGENOM; CLU_044458_1_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:0004177; F:aminopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   InterPro; IPR016117; ArgJ-like_dom_sf.
DR   InterPro; IPR005321; Peptidase_S58_DmpA.
DR   PANTHER; PTHR36512; PTHR36512; 1.
DR   Pfam; PF03576; Peptidase_S58; 1.
DR   SUPFAM; SSF56266; SSF56266; 1.
PE   3: Inferred from homology;
KW   Aminopeptidase; Cell membrane; Hydrolase; Membrane; Protease;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           1..344
FT                   /note="Uncharacterized aminopeptidase MT1375"
FT                   /id="PRO_0000427379"
FT   TRANSMEM        25..45
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        68..88
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        104..124
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        133..153
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        161..181
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        224..244
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        276..296
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        302..322
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   344 AA;  33953 MW;  296A055FECF8E650 CRC64;
     MNSITDVGGI RVGHYQRLDP DASLGAGWAC GVTVVLPPPG TVGAVDCRGG APGTRETDLL
     DPANSVRFVD ALLLAGGSAY GLAAADGVMR WLEEHRRGVA MDSGVVPIVP GAVIFDLPVG
     GWNCRPTADF GYSACAAAGV DVAVGTVGVG VGARAGALKG GVGTASATLQ SGVTVGVLAV
     VNAAGNVVDP ATGLPWMADL VGEFALRAPP AEQIAALAQL SSPLGAFNTP FNTTIGVIAC
     DAALSPAACR RIAIAAHDGL ARTIRPAHTP LDGDTVFALA TGAVAVPPEA GVPAALSPET
     QLVTAVGAAA ADCLARAVLA GVLNAQPVAG IPTYRDMFPG AFGS