TTFA_MYCS2
ID TTFA_MYCS2 Reviewed; 278 AA.
AC A0QQF4; I7F6I5;
DT 02-JUN-2021, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2007, sequence version 1.
DT 25-MAY-2022, entry version 89.
DE RecName: Full=Trehalose monomycolate transport factor A {ECO:0000303|PubMed:31239378, ECO:0000303|PubMed:31833106};
DE AltName: Full=TMM transport factor A {ECO:0000303|PubMed:31239378, ECO:0000303|PubMed:31833106};
GN Name=ttfA {ECO:0000303|PubMed:31239378, ECO:0000303|PubMed:31833106};
GN OrderedLocusNames=MSMEG_0736 {ECO:0000303|PubMed:31239378,
GN ECO:0000303|PubMed:31833106, ECO:0000312|EMBL:ABK72891.1},
GN MSMEI_0720 {ECO:0000312|EMBL:AFP37200.1};
OS Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium
OS smegmatis).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycolicibacterium.
OX NCBI_TaxID=246196 {ECO:0000312|EMBL:ABK72891.1};
RN [1] {ECO:0000312|EMBL:ABK72891.1, ECO:0000312|Proteomes:UP000000757}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700084 / mc(2)155 {ECO:0000312|Proteomes:UP000000757};
RA Fleischmann R.D., Dodson R.J., Haft D.H., Merkel J.S., Nelson W.C.,
RA Fraser C.M.;
RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000312|EMBL:AFP37200.1, ECO:0000312|Proteomes:UP000006158}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700084 / mc(2)155 {ECO:0000312|Proteomes:UP000006158};
RX PubMed=17295914; DOI=10.1186/gb-2007-8-2-r20;
RA Deshayes C., Perrodou E., Gallien S., Euphrasie D., Schaeffer C.,
RA Van-Dorsselaer A., Poch O., Lecompte O., Reyrat J.-M.;
RT "Interrupted coding sequences in Mycobacterium smegmatis: authentic
RT mutations or sequencing errors?";
RL Genome Biol. 8:R20.1-R20.9(2007).
RN [3] {ECO:0000312|EMBL:AFP37200.1, ECO:0000312|Proteomes:UP000006158}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700084 / mc(2)155 {ECO:0000312|Proteomes:UP000006158};
RX PubMed=18955433; DOI=10.1101/gr.081901.108;
RA Gallien S., Perrodou E., Carapito C., Deshayes C., Reyrat J.-M.,
RA Van Dorsselaer A., Poch O., Schaeffer C., Lecompte O.;
RT "Ortho-proteogenomics: multiple proteomes investigation through orthology
RT and a new MS-based protocol.";
RL Genome Res. 19:128-135(2009).
RN [4]
RP FUNCTION, INTERACTION WITH MMPL3 AND MSMEG_5308, SUBCELLULAR LOCATION,
RP DOMAIN, IDENTIFICATION BY MASS SPECTROMETRY, DISRUPTION PHENOTYPE,
RP TOPOLOGY, AND MUTAGENESIS OF 1-MET--ASP-23; 24-ILE--ARG-278;
RP 51-ASP--ARG-278; 101-GLY--ARG-278; 151-PHE--ARG-278 AND 206-GLY--ARG-278.
RC STRAIN=ATCC 700084 / mc(2)155 {ECO:0000303|PubMed:31239378};
RX PubMed=31239378; DOI=10.1128/mbio.00850-19;
RA Fay A., Czudnochowski N., Rock J.M., Johnson J.R., Krogan N.J.,
RA Rosenberg O., Glickman M.S.;
RT "Two Accessory Proteins Govern MmpL3 Mycolic Acid Transport in
RT Mycobacteria.";
RL MBio 10:E00850-E00850(2019).
RN [5] {ECO:0007744|PDB:6T84}
RP X-RAY CRYSTALLOGRAPHY (1.40 ANGSTROMS) OF 24-205, AND SUBUNIT.
RC STRAIN=ATCC 700084 / mc(2)155 {ECO:0000303|PubMed:31833106};
RX PubMed=31833106; DOI=10.1002/prot.25863;
RA Ung K.L., Alsarraf H.M.A.B., Kremer L., Blaise M.;
RT "The crystal structure of the mycobacterial trehalose monomycolate
RT transport factor A, TtfA, reveals an atypical fold.";
RL Proteins 88:809-815(2020).
CC -!- FUNCTION: Required for MmpL3-dependent trehalose monomycolate (TMM)
CC transport to the cell wall. Required for growth and cell elongation.
CC {ECO:0000269|PubMed:31239378}.
CC -!- SUBUNIT: Monomer (PubMed:31833106). Interacts (via N-terminus) with
CC MmpL3; active trehalose monomycolate (TMM) biosynthesis is not required
CC for the complex formation. Interacts with MSMEG_5308 (PubMed:31239378).
CC {ECO:0000269|PubMed:31239378, ECO:0000269|PubMed:31833106}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000269|PubMed:31239378}; Single-pass membrane protein
CC {ECO:0000255}. Cell septum {ECO:0000269|PubMed:31239378}. Cell tip
CC {ECO:0000269|PubMed:31239378}. Note=Colocalizes with MmpL3 to the cell
CC poles and septa. Trehalose monomycolate (TMM) synthesis is not required
CC for localization to the poles or septa. {ECO:0000269|PubMed:31239378}.
CC -!- DOMAIN: The N-terminal domain (1-205) is necessary and sufficient for
CC proper localization and function of this protein, and for its
CC interaction with MmpL3. {ECO:0000269|PubMed:31239378}.
CC -!- DISRUPTION PHENOTYPE: Knockdown of this gene leads to cessation of
CC growth and shorter misshapen cells. Accummulation of trehalose
CC monomycolate (TMM) and lack of trehalose dimycolate (TDM). Accumulates
CC MSMEG_5308 protein. {ECO:0000269|PubMed:31239378}.
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DR EMBL; CP000480; ABK72891.1; -; Genomic_DNA.
DR EMBL; CP001663; AFP37200.1; -; Genomic_DNA.
DR RefSeq; WP_003892156.1; NZ_SIJM01000036.1.
DR RefSeq; YP_885142.1; NC_008596.1.
DR PDB; 6T84; X-ray; 1.40 A; A=24-205.
DR PDBsum; 6T84; -.
DR AlphaFoldDB; A0QQF4; -.
DR SMR; A0QQF4; -.
DR STRING; 246196.MSMEI_0720; -.
DR PRIDE; A0QQF4; -.
DR EnsemblBacteria; ABK72891; ABK72891; MSMEG_0736.
DR EnsemblBacteria; AFP37200; AFP37200; MSMEI_0720.
DR GeneID; 66738911; -.
DR KEGG; msg:MSMEI_0720; -.
DR KEGG; msm:MSMEG_0736; -.
DR PATRIC; fig|246196.19.peg.732; -.
DR eggNOG; ENOG502ZNE6; Bacteria.
DR OMA; GRVRQIW; -.
DR OrthoDB; 1522270at2; -.
DR Proteomes; UP000000757; Chromosome.
DR Proteomes; UP000006158; Chromosome.
DR GO; GO:0030428; C:cell septum; IEA:UniProtKB-SubCell.
DR GO; GO:0051286; C:cell tip; IEA:UniProtKB-SubCell.
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:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0006869; P:lipid transport; IEA:UniProtKB-KW.
PE 1: Evidence at protein level;
KW 3D-structure; Cell inner membrane; Cell membrane;
KW Cell wall biogenesis/degradation; Lipid transport; Membrane;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..278
FT /note="Trehalose monomycolate transport factor A"
FT /id="PRO_0000452603"
FT TOPO_DOM 1
FT /note="Periplasmic"
FT /evidence="ECO:0000305|PubMed:31239378"
FT TRANSMEM 2..22
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 23..278
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:31239378"
FT REGION 200..278
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 250..278
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 1..23
FT /note="Missing: No localization to poles or septa, loss of
FT function complementation and interaction with MmpL3."
FT /evidence="ECO:0000269|PubMed:31239378"
FT MUTAGEN 24..278
FT /note="Missing: No localization to poles or septa, loss of
FT function complementation and interaction with MmpL3."
FT /evidence="ECO:0000269|PubMed:31239378"
FT MUTAGEN 51..278
FT /note="Missing: No localization to poles or septa, loss of
FT function complementation and interaction with MmpL3."
FT /evidence="ECO:0000269|PubMed:31239378"
FT MUTAGEN 101..278
FT /note="Missing: No localization to poles or septa, loss of
FT function complementation and interaction with MmpL3."
FT /evidence="ECO:0000269|PubMed:31239378"
FT MUTAGEN 151..278
FT /note="Missing: No localization to poles or septa, loss of
FT function complementation and interaction with MmpL3."
FT /evidence="ECO:0000269|PubMed:31239378"
FT MUTAGEN 206..278
FT /note="Missing: Localizes to poles and septa in a pattern
FT similar to the wild-type. Complements function. Interacts
FT with MmpL3."
FT /evidence="ECO:0000269|PubMed:31239378"
FT HELIX 30..41
FT /evidence="ECO:0007829|PDB:6T84"
FT STRAND 44..51
FT /evidence="ECO:0007829|PDB:6T84"
FT HELIX 52..55
FT /evidence="ECO:0007829|PDB:6T84"
FT HELIX 59..61
FT /evidence="ECO:0007829|PDB:6T84"
FT STRAND 69..77
FT /evidence="ECO:0007829|PDB:6T84"
FT STRAND 80..87
FT /evidence="ECO:0007829|PDB:6T84"
FT TURN 88..90
FT /evidence="ECO:0007829|PDB:6T84"
FT STRAND 91..97
FT /evidence="ECO:0007829|PDB:6T84"
FT STRAND 106..110
FT /evidence="ECO:0007829|PDB:6T84"
FT STRAND 122..127
FT /evidence="ECO:0007829|PDB:6T84"
FT STRAND 130..135
FT /evidence="ECO:0007829|PDB:6T84"
FT HELIX 137..143
FT /evidence="ECO:0007829|PDB:6T84"
FT HELIX 146..154
FT /evidence="ECO:0007829|PDB:6T84"
FT STRAND 161..164
FT /evidence="ECO:0007829|PDB:6T84"
FT STRAND 166..173
FT /evidence="ECO:0007829|PDB:6T84"
FT HELIX 179..195
FT /evidence="ECO:0007829|PDB:6T84"
FT HELIX 196..198
FT /evidence="ECO:0007829|PDB:6T84"
SQ SEQUENCE 278 AA; 31196 MW; B5CD4F2D3C2A7517 CRC64;
MVPLWFTLSA LCFVGAAVLL YVDIDRRRGL GRRRKSWAKS HGFDYEYESE DLLKRWKRGV
MSTVGDVTAK NVVLGQIRGE AVFIFDIEEV ATVIALHRKV GTNVVVDLRL KGLKEPREND
IWLLGAIGPR MVYSTNLDAA RRACDRRMVT FAHTAPDCAE IMWNEQNWTL VAMPVTSNRA
QWDEGLRTVR QFNDLLRVLP PVPQNGSQAA LPRRGGSPSR PLAPTPAGRR ELPPGRADVP
PARGDVSRFA PRPEAGRSDA FRRPPPARNG REASHFQR
