ID A0A0M2JNX7_9MYCO Unreviewed; 360 AA.
AC A0A0M2JNX7;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE SubName: Full=Molecular chaperone {ECO:0000313|EMBL:KKE98148.1};
DE Flags: Fragment;
GN ORFNames=WN67_30815 {ECO:0000313|EMBL:KKE98148.1};
OS Mycolicibacterium obuense.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycolicibacterium.
OX NCBI_TaxID=1807 {ECO:0000313|EMBL:KKE98148.1, ECO:0000313|Proteomes:UP000034150};
RN [1] {ECO:0000313|EMBL:KKE98148.1, ECO:0000313|Proteomes:UP000034150}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UC1 {ECO:0000313|EMBL:KKE98148.1,
RC ECO:0000313|Proteomes:UP000034150};
RA Greninger A.L., Cunningham G., Chiu C.Y., Miller S.;
RT "Genome sequence of Mycobacterium obuense UC1.";
RL Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC -!- SIMILARITY: Belongs to the heat shock protein 70 family.
CC {ECO:0000256|ARBA:ARBA00007381}.
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:KKE98148.1}.
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; LAUZ02000228; KKE98148.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0M2JNX7; -.
DR STRING; 1807.MOBUDSM44075_00018; -.
DR PATRIC; fig|1807.13.peg.6417; -.
DR OrthoDB; 5173286at2; -.
DR Proteomes; UP000034150; 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; IPR018181; Heat_shock_70_CS.
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 SUPFAM; SSF53067; Actin-like ATPase domain; 1.
DR PROSITE; PS01036; HSP70_3; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 296..317
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT REGION 261..288
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 319..360
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 322..349
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KKE98148.1"
FT NON_TER 360
FT /evidence="ECO:0000313|EMBL:KKE98148.1"
SQ SEQUENCE 360 AA; 37155 MW; E4F47F32EB5B3926 CRC64;
PPRLIPDALA ALTAMVADPG LERRGVLAVL DIGGSGTSIS LAEAGSLELI GRTERFAEFA
GDQIDQALLT HVLERVPHSG EDTGATAAVG SLARLREQCR SAKERLSTET EARIDVDVPG
YRGEIVVTRA DLESLLARPL DDVIEALRDT LQRNNTGSAA LSAVVLVGGG SAIPAVRQRF
SSYPGRVLWS PRPALDAAVG AALFAAFGGA AETATRAAPA VAPAGADADA TYALAWSQDD
PSTEDVVPYA GEDTYVIDDY ADDATGRAER PNPYRLSDPQ ESPAEDEPVG WRRLPLSLLG
VVAAIALVAV GGVAIALTSV DGSDSDRPTP GNSPLSRELT PTTAAGETVT VPGQPAAPPT
//
