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Database: UniProt
Entry: A0A0S8FJJ9_9GAMM
LinkDB: A0A0S8FJJ9_9GAMM
Original site: A0A0S8FJJ9_9GAMM 
ID   A0A0S8FJJ9_9GAMM        Unreviewed;       510 AA.
AC   A0A0S8FJJ9;
DT   17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT   17-FEB-2016, sequence version 1.
DT   27-MAR-2024, entry version 30.
DE   SubName: Full=ATP-dependent protease {ECO:0000313|EMBL:KPK60927.1};
GN   ORFNames=AMJ59_04460 {ECO:0000313|EMBL:KPK60927.1};
OS   Gammaproteobacteria bacterium SG8_31.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria.
OX   NCBI_TaxID=1703405 {ECO:0000313|EMBL:KPK60927.1, ECO:0000313|Proteomes:UP000051321};
RN   [1] {ECO:0000313|EMBL:KPK60927.1, ECO:0000313|Proteomes:UP000051321}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SG8_31 {ECO:0000313|EMBL:KPK60927.1};
RX   PubMed=25922666; DOI=10.1186/s40168-015-0077-6;
RA   Baker B.J., Lazar C.S., Teske A.P., Dick G.J.;
RT   "Genomic resolution of linkages in carbon, nitrogen, and sulfur cycling
RT   among widespread estuary sediment bacteria.";
RL   Microbiome 3:14-14(2015).
CC   -!- SIMILARITY: Belongs to the Mg-chelatase subunits D/I family. ComM
CC       subfamily. {ECO:0000256|ARBA:ARBA00006354}.
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:KPK60927.1}.
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DR   EMBL; LJTI01000004; KPK60927.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0S8FJJ9; -.
DR   PATRIC; fig|1703405.3.peg.1755; -.
DR   Proteomes; UP000051321; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0008233; F:peptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0032508; P:DNA duplex unwinding; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.230.10; -; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR045006; CHLI-like.
DR   InterPro; IPR001208; MCM_dom.
DR   InterPro; IPR004482; Mg_chelat-rel.
DR   InterPro; IPR025158; Mg_chelat-rel_C.
DR   InterPro; IPR000523; Mg_chelatse_chII-like_cat_dom.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR020568; Ribosomal_Su5_D2-typ_SF.
DR   InterPro; IPR014721; Ribsml_uS5_D2-typ_fold_subgr.
DR   NCBIfam; TIGR00368; YifB family Mg chelatase-like AAA ATPase; 1.
DR   PANTHER; PTHR32039:SF7; COMPETENCE PROTEIN COMM; 1.
DR   PANTHER; PTHR32039; MAGNESIUM-CHELATASE SUBUNIT CHLI; 1.
DR   Pfam; PF13541; ChlI; 1.
DR   Pfam; PF01078; Mg_chelatase; 1.
DR   Pfam; PF13335; Mg_chelatase_C; 1.
DR   PRINTS; PR01657; MCMFAMILY.
DR   SMART; SM00382; AAA; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF54211; Ribosomal protein S5 domain 2-like; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Hydrolase {ECO:0000313|EMBL:KPK60927.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Protease {ECO:0000313|EMBL:KPK60927.1}.
FT   DOMAIN          212..394
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
FT   REGION          490..510
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   510 AA;  54083 MW;  BEA1A7422C8AEFB9 CRC64;
     MGLAKVASRA YLGIAAPPVS VEVDLAGGLP ALSIVGLPEA TVRESKDRVR AALRNCGFDF
     PPRRITVNLA PADLPKSGGR FDLPIALGVL AASGQLPSES LRGMEFIGEL SLDGRLRAVE
     GSLSAAAAAS AERVTLIVPR GNMEEVLLVR DASLIAAGHL MSVWKHLAGH EELPPVVRGP
     ASSCQSPPAN GDLAEVRGQP TARRALEIAA CGGHDMLMVG PPGTGKSMLA KRLPGLLPPL
     ADAEALDVAL VTAARDGRFA AADWGRRPFR QPHHTATISA LVGGGSVPRP GEVSLAHRGV
     LFMDELPEFP RGVLDALRQP LEDREVTISR ARGRLTFPAD FQLVAAMNPC PCGYFGDSFE
     ACRCTPDAIR RYQGRISGPL MDRLDLRIDL VRPSAAILVD DAGEETSHTV AQRVLEARAR
     QQRRGFLNAR IPPEMLVGLC QPTEAALALL CTSAERFHLS ARACHRVLRV ARTIADLAGR
     SGIEAGDISE AVSRRPHASR AGRPRSAALS
//
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