ID A0A1X1UXS5_9MYCO Unreviewed; 614 AA.
AC A0A1X1UXS5;
DT 05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2017, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=Molecular chaperone {ECO:0008006|Google:ProtNLM};
GN ORFNames=AWC06_12180 {ECO:0000313|EMBL:ORV61622.1};
OS Mycobacterium fragae.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycobacterium.
OX NCBI_TaxID=1260918 {ECO:0000313|EMBL:ORV61622.1, ECO:0000313|Proteomes:UP000194000};
RN [1] {ECO:0000313|EMBL:ORV61622.1, ECO:0000313|Proteomes:UP000194000}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 45731 {ECO:0000313|EMBL:ORV61622.1,
RC ECO:0000313|Proteomes:UP000194000};
RA Tarcisio F., Conor M., Antonella G., Elisabetta G., Giulia F.S., Sara T.,
RA Anna F., Clotilde B., Roberto B., Veronica D.S., Fabio R., Monica P.,
RA Olivier J., Enrico T., Nicola S.;
RT "The new phylogeny of the genus Mycobacterium.";
RL Submitted (JAN-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:ORV61622.1}.
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DR EMBL; LQOW01000015; ORV61622.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1X1UXS5; -.
DR STRING; 1260918.AWC06_12180; -.
DR OrthoDB; 5173286at2; -.
DR Proteomes; UP000194000; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0140662; F:ATP-dependent protein folding chaperone; IEA:InterPro.
DR Gene3D; 3.30.420.40; -; 2.
DR InterPro; IPR043129; ATPase_NBD.
DR InterPro; IPR013126; Hsp_70_fam.
DR PANTHER; PTHR42749; CELL SHAPE-DETERMINING PROTEIN MREB; 1.
DR PANTHER; PTHR42749:SF1; CELL SHAPE-DETERMINING PROTEIN MREB; 1.
DR Pfam; PF00012; HSP70; 1.
DR PRINTS; PR00301; HEATSHOCK70.
DR SUPFAM; SSF53067; Actin-like ATPase domain; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000194000};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 452..472
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT REGION 421..442
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 479..577
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 589..614
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 479..494
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 495..538
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 539..577
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 614 AA; 62909 MW; 4FFFE918800C022E CRC64;
MYDPLGLSIG TSNFVAVRNG TPPVMRRAVL TLFPNRPPEL GVPAEDLNPS DTGTLMAGFV
ERVGGSTALA SADGTTHDPA LLLVEALDAM IGLTGGDAPG SNITIAVPAH WGPEALRALQ
DALRTHSGFV GSGIPPRLVS DAVTALTALN SGARLPAEGV VGLLDFGAGG TNITLTDAAS
GFTPIADTMR CPQFSGDLID QALLVHVLDH IGHTGGGDPA STAVVGQFAG LREECRRAKE
QLSDETVTEL VAELPGHSSR VTVTRAELES LVERQLVDVF SAFDAMLRRN KVRRKGLAAL
AMAGGGARIP LVAQRLSAHA KTSVVTAVQP AHAMAVGAVM LASRGPGRHE EIEAPTSATA
MAGAVTGSFA ASTGTFSAPT GGFGASGLDS FVGEDPSETL HQLAWSEADA GNDPVFYTGE
PYDLDGGATP SQRLLKVEPP DEPRRRYRLP QLLFGLVALI SMIAIGGVAF TLTSATDHQA
PPATGSTTVV PPLPASSKLP SPSPLPPPPS AAPSPSVAPP PTSVEPPPPP PPPVTTTYRP
PTTSQQATTS TTTTTTTTTT TTTPPPSTTT TTTTTVPMTT TYLNLPFVPV PIPVQVPGGQ
GSPNQPGLPN QPGF
//
