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Database: UniProt
Entry: A0A0R2U6P1_9GAMM
LinkDB: A0A0R2U6P1_9GAMM
Original site: A0A0R2U6P1_9GAMM 
ID   A0A0R2U6P1_9GAMM        Unreviewed;       502 AA.
AC   A0A0R2U6P1;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   08-NOV-2023, entry version 20.
DE   SubName: Full=ATP-dependent protease {ECO:0000313|EMBL:KRO95231.1};
GN   ORFNames=ABS24_07805 {ECO:0000313|EMBL:KRO95231.1};
OS   SAR92 bacterium BACL26 MAG-121220-bin70.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Cellvibrionales;
OC   Porticoccaceae; SAR92 clade.
OX   NCBI_TaxID=1655626 {ECO:0000313|EMBL:KRO95231.1, ECO:0000313|Proteomes:UP000051213};
RN   [1] {ECO:0000313|EMBL:KRO95231.1, ECO:0000313|Proteomes:UP000051213}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BACL26 MAG-121220-bin70 {ECO:0000313|EMBL:KRO95231.1};
RA   Hugerth L.W., Larsson J., Alneberg J., Lindh M.V., Legrand C., Pinhassi J.,
RA   Andersson A.F.;
RT   "Metagenome-Assembled Genomes uncover a global brackish microbiome.";
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
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:KRO95231.1}.
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DR   EMBL; LICA01000099; KRO95231.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0R2U6P1; -.
DR   Proteomes; UP000051213; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0008233; F:peptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd00009; AAA; 1.
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; 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   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   Hydrolase {ECO:0000313|EMBL:KRO95231.1};
KW   Protease {ECO:0000313|EMBL:KRO95231.1}.
FT   DOMAIN          209..388
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
SQ   SEQUENCE   502 AA;  55029 MW;  EC5F3A586F0D7840 CRC64;
     MSLAVIKSRA KLGIEAPIIS VEVHLSNGLP AFNIVGLPEA SVKESKDRVR SAIINSHFEF
     PARRITVNLA PADIPKQGSR FDLAIAIGIL VASGQVPSDR VKDYEFIGEL ALTGDIRPVD
     ALLPSAQRCS EADNQLIIAK ENAHEASLVE SLAVLPANHL LEVSAHLHGR ETIELWLRED
     RVLTESTEEL SDIIGQQHAK RAMEIAATGG HHLLFYGPPG TGKTMLASRL AGILPPLSNQ
     EALEVASIHS VAGKGLRQNI WLRPFRSPHH TASAAALVGG GGIPKPGEIS LAHHGVLFLD
     ELPEFSRNVL EVLREPLESG QIMISRVNAQ TLYPAKFQLI AAMNPCPCGH LGSNRCVCPL
     DQITRYQNKI SGPLLDRIDL QVQVSAITNH QLLSQETIAK GETNQQIQTR VCAARYLQIE
     RQGKINADLS SQELREVCPL NKEQKSLMNQ AIDQFALSTR GFYRVLKVAR TLADLEKISY
     PEIPHYQEAL SYRSTMDRRA SD
//
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