Y1842_MYCTO
ID Y1842_MYCTO Reviewed; 455 AA.
AC P9WFP2; L0T820; P95166; Q50592;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 25-MAY-2022, entry version 42.
DE RecName: Full=UPF0053 protein MT1890;
GN OrderedLocusNames=MT1890;
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}.
CC -!- SIMILARITY: Belongs to the UPF0053 family. {ECO:0000305}.
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; AAK46161.1; -; Genomic_DNA.
DR PIR; B70664; B70664.
DR RefSeq; WP_003917539.1; NZ_KK341227.1.
DR AlphaFoldDB; P9WFP2; -.
DR SMR; P9WFP2; -.
DR EnsemblBacteria; AAK46161; AAK46161; MT1890.
DR KEGG; mtc:MT1890; -.
DR PATRIC; fig|83331.31.peg.2034; -.
DR HOGENOM; CLU_015237_4_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:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR CDD; cd04590; CBS_pair_CorC_HlyC_assoc; 1.
DR Gene3D; 3.10.580.10; -; 1.
DR Gene3D; 3.30.465.10; -; 1.
DR InterPro; IPR000644; CBS_dom.
DR InterPro; IPR046342; CBS_dom_sf.
DR InterPro; IPR002550; CNNM.
DR InterPro; IPR036318; FAD-bd_PCMH-like_sf.
DR InterPro; IPR016169; FAD-bd_PCMH_sub2.
DR InterPro; IPR044751; Ion_transp-like_CBS.
DR InterPro; IPR005170; Transptr-assoc_dom.
DR Pfam; PF00571; CBS; 2.
DR Pfam; PF03471; CorC_HlyC; 1.
DR Pfam; PF01595; DUF21; 1.
DR SMART; SM01091; CorC_HlyC; 1.
DR SUPFAM; SSF54631; SSF54631; 1.
DR SUPFAM; SSF56176; SSF56176; 1.
DR PROSITE; PS51371; CBS; 2.
DR PROSITE; PS51846; CNNM; 1.
PE 3: Inferred from homology;
KW CBS domain; Cell membrane; Membrane; Repeat; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..455
FT /note="UPF0053 protein MT1890"
FT /id="PRO_0000428504"
FT TRANSMEM 6..26
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 68..88
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 106..126
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 148..168
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 2..205
FT /note="CNNM transmembrane"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01193"
FT DOMAIN 224..285
FT /note="CBS 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00703"
FT DOMAIN 286..346
FT /note="CBS 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00703"
SQ SEQUENCE 455 AA; 48154 MW; 49F6BEC2B50B3B0C CRC64;
MNLTDTVATI LAILALTAGT GVFVAAEFSL TALDRSTVEA NARGGTSRDR FIQRAHHRLS
FQLSGAQLGI SITTLATGYL TEPLVAELPH PGLVAVGMSD RVADGLITFF ALVIVTSLSM
VFGELVPKYL AVARPLRTAR SVVAGQVLFS LLLTPAIRLT NGAANWIVRR LGIEPAEELR
SARTPQELVS LVRSSARSGA LDDATAWLMR RSLQFGALTA EELMTPRSKI VALQTDDTIA
DLVAAAAASG FSRFPVVEGD LDATVGIVHV KQVFEVPPGD RAHTLLTTVA EPVAVVPSTL
DGDAVMAQVR ASALQTAMVV DEYGGTAGMV TLEDLIEEIV GDVRDEHDDA TPDVVAAGNG
WRVSGLLRID EVASATGYRA PDGPYETISG LVLRELGHIP VAGETVELTA LDQDGLPDDS
MRWLATVIQM DGRRIDLLEL IKMGGHADPG SGRGR