ID A0A1A0M587_9MYCO Unreviewed; 565 AA.
AC A0A1A0M587;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE SubName: Full=Molecular chaperone {ECO:0000313|EMBL:OBA80547.1};
GN ORFNames=A9W99_17165 {ECO:0000313|EMBL:OBA80547.1};
OS Mycobacterium sp. 1164966.3.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycobacterium.
OX NCBI_TaxID=1856861 {ECO:0000313|EMBL:OBA80547.1, ECO:0000313|Proteomes:UP000092060};
RN [1] {ECO:0000313|Proteomes:UP000092060}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1164966.3 {ECO:0000313|Proteomes:UP000092060};
RA Sutton G., Brinkac L., Sanka R., Adams M., Lau E., Garcia-Basteiro A.,
RA Lopez-Varela E., Palencia S.;
RL Submitted (JUN-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:OBA80547.1}.
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DR EMBL; LZSG01000042; OBA80547.1; -; Genomic_DNA.
DR RefSeq; WP_067379437.1; NZ_LZSG01000042.1.
DR AlphaFoldDB; A0A1A0M587; -.
DR STRING; 1856861.A9W99_17165; -.
DR OrthoDB; 5173286at2; -.
DR Proteomes; UP000092060; 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 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:UP000092060};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 434..456
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT REGION 384..425
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 459..565
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 464..490
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 491..505
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 506..552
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 565 AA; 57630 MW; E7620D3A6901665B CRC64;
MSEPLGLSIG VANLVAVRAG GTPVTRSSVL TLYDDQPTEV GLPEENPNLT KPGLVMRGFV
ERVGDRNPLV AADGTKYLGD ALMVEALEAL ARTVGYGSPI TIAVPAYWSE AQSAAVRTEF
FAQPGLAAEG VTPVLISDAA AGLAALRTKP GFPRDGVVAL CDFGAGGTSV TLINASSNFQ
QIGPSVRYSN FSGESIDQLI ANYVRSGGQD AATSTNVAAA GRPAPPTLLG ECRRAKEQLS
SGTTATIATG QGADFRLSRT ELEHLISAPL DQFLATLAEV LQRNGIPHAG LAAVAVLGGG
ASIPLITARL SERLRVPVLT TLEPMFSAAI GAAALGSQHL SAGAATAAGA AVELPTELVG
TPETTALRNQ DADTDKPTYA LAWSQDSATG EEPIPYTGPE HSGGYGVEPT AQATGPEDRH
TAEPGPLPWY KRTALVVSVA AALAAVLLAV VLALTVGHGK TTPKEPAPSQ TPQTVTITGP
NNSPTTTVIQ PPPASSQPPA TTTAQPPPTT TAATTTTQPP TTTTTQRTTS SQATTTSSQA
PSSSTQRTTT APPTPPTRRP FGPAG
//
