ID   A6VWZ8_MARMS            Unreviewed;       906 AA.
AC   A6VWZ8;
DT   21-AUG-2007, integrated into UniProtKB/TrEMBL.
DT   21-AUG-2007, sequence version 1.
DT   27-MAR-2024, entry version 85.
DE   SubName: Full=Molecular chaperone {ECO:0000313|EMBL:ABR70977.1};
GN   OrderedLocusNames=Mmwyl1_2055 {ECO:0000313|EMBL:ABR70977.1};
OS   Marinomonas sp. (strain MWYL1).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC   Oceanospirillaceae; Marinomonas.
OX   NCBI_TaxID=400668 {ECO:0000313|EMBL:ABR70977.1};
RN   [1] {ECO:0000313|EMBL:ABR70977.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MWYL1 {ECO:0000313|EMBL:ABR70977.1};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Kiss H., Brettin T., Bruce D., Detter J.C., Han C.,
RA   Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E.,
RA   Johnston A.W.B., Todd J.D., Rogers R., Wexler M., Bond P.L., Li Y.,
RA   Richardson P.;
RT   "Complete sequence of Marinomonas sp. MWYL1.";
RL   Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the heat shock protein 70 family.
CC       {ECO:0000256|ARBA:ARBA00007381}.
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DR   EMBL; CP000749; ABR70977.1; -; Genomic_DNA.
DR   AlphaFoldDB; A6VWZ8; -.
DR   STRING; 400668.Mmwyl1_2055; -.
DR   KEGG; mmw:Mmwyl1_2055; -.
DR   eggNOG; COG0443; Bacteria.
DR   HOGENOM; CLU_013948_0_0_6; -.
DR   OrthoDB; 580874at2; -.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0140662; F:ATP-dependent protein folding chaperone; IEA:InterPro.
DR   CDD; cd10170; HSP70_NBD; 1.
DR   Gene3D; 3.30.420.40; -; 2.
DR   InterPro; IPR043129; ATPase_NBD.
DR   InterPro; IPR021030; DUF3731.
DR   InterPro; IPR018181; Heat_shock_70_CS.
DR   InterPro; IPR013126; Hsp_70_fam.
DR   PANTHER; PTHR19375; HEAT SHOCK PROTEIN 70KDA; 1.
DR   PANTHER; PTHR19375:SF184; STRESS-70 PROTEIN, MITOCHONDRIAL; 1.
DR   Pfam; PF12531; DUF3731; 1.
DR   Pfam; PF00012; HSP70; 1.
DR   PRINTS; PR00301; HEATSHOCK70.
DR   SUPFAM; SSF53067; Actin-like ATPase domain; 2.
DR   PROSITE; PS00297; HSP70_1; 1.
DR   PROSITE; PS00329; HSP70_2; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Chaperone {ECO:0000256|ARBA:ARBA00023186};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741}.
SQ   SEQUENCE   906 AA;  99658 MW;  97884BD929EDCE1A CRC64;
     MAQPAFHSAY RVGIDLGTTN CVVSYVPVAD HSNANAPALL PIPQVMADGS VQEFTYLPSA
     IYVLASDEIG KIDPVLPWRH HDKERIVGVG ALALGQRRAG QLVQSAKSWL SHRQVDRRSA
     ILPWASEFPK KLSPLEASKI LLLHIKQSWN HRFADAPLES QSIALTLPAS FDEEARALTL
     EAAKLAGLND LYLLEEPQAA CYHYISDDEK LAALVDKKML LVVDIGGGTS DFSLVAIQPT
     SAKAKSVSLK RIAVGEHLLL GGDNLDQALA FQLDPKQISA LSATRLAALV QQTRQAKETL
     LGKDAPESLS ITVLGGGSRL IGGSQKFDVS REALLEQIRN GFFPLVKSDD KVQKSDYAMH
     TLGLPYESDP AFTRHLAAFL QQHGAVIEAA TGSIMPDAVL FNGGLFNSPV LKARLLEQLN
     TWSSKPILAC SADEPNDAVA KGAAMYLNAL AGESTRIESG VAHSLYLKVG ENEFVGILPK
     GTLKGETIRL EQEFFVTLGQ QVQFPLYRSD DHLECVVGRV RDQDGLHYIS TLMTELDGSI
     DSQETAVTLS VQMTEVGVLQ VVLNANNQKD QWRLDFSTQA SSSQDSEQSD ESGLLHANMG
     QAEEHLAKCF SSAGQKQNPD LVKSLKQDLE QLLGNRDDWN LATSRRLVDK LLSLKSGRTK
     SAQHERQWLQ LMGYCLRPGF GAADDLARVQ QVVNATKAGA QFDTAPVWGQ YWTLYRRIAG
     GLSIEQQTYL FKQFSQYYSP TGQRSRDKMK ALTTKSSDDL IRLVGALESL SNEDKTTAID
     WLLKRLQKTS EPDTAWWTIG RIASRHLLSG KQEQRIAENK LFPILEVTLK EDWKKRKQAG
     LAAVLMSQVS VGESDKLSAL RKKVANKLKK DKCPAQWLER LESQIEINSD ELNALVGESL
     PIGLRL
//