ID A0A0T0M908_9FLAO Unreviewed; 403 AA.
AC A0A0T0M908;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=ATPase {ECO:0000313|EMBL:KQS92750.1};
GN ORFNames=ASG21_10015 {ECO:0000313|EMBL:KQS92750.1};
OS Chryseobacterium sp. Leaf394.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales; Weeksellaceae;
OC Chryseobacterium group; Chryseobacterium.
OX NCBI_TaxID=1736361 {ECO:0000313|EMBL:KQS92750.1, ECO:0000313|Proteomes:UP000051822};
RN [1] {ECO:0000313|EMBL:KQS92750.1, ECO:0000313|Proteomes:UP000051822}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf394 {ECO:0000313|EMBL:KQS92750.1,
RC ECO:0000313|Proteomes:UP000051822};
RX PubMed=26633631; DOI=.1038/nature16192;
RA Bai Y., Muller D.B., Srinivas G., Garrido-Oter R., Potthoff E., Rott M.,
RA Dombrowski N., Munch P.C., Spaepen S., Remus-Emsermann M., Huttel B.,
RA McHardy A.C., Vorholt J.A., Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiota.";
RL Nature 528:364-369(2015).
RN [2] {ECO:0000313|Proteomes:UP000051822}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf394 {ECO:0000313|Proteomes:UP000051822};
RA Garrido-Oter R., Mueller D.B.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|Proteomes:UP000051822}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf394 {ECO:0000313|Proteomes:UP000051822};
RA Vorholt J.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
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:KQS92750.1}.
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DR EMBL; LMQH01000011; KQS92750.1; -; Genomic_DNA.
DR RefSeq; WP_056080654.1; NZ_LMQH01000011.1.
DR AlphaFoldDB; A0A0T0M908; -.
DR STRING; 1736361.ASG21_10015; -.
DR OrthoDB; 1195727at2; -.
DR Proteomes; UP000051822; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003824; F:catalytic activity; IEA:UniProt.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR Gene3D; 3.40.50.20; -; 1.
DR Gene3D; 3.30.1490.20; ATP-grasp fold, A domain; 1.
DR Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 1.
DR InterPro; IPR011761; ATP-grasp.
DR InterPro; IPR013815; ATP_grasp_subdomain_1.
DR PANTHER; PTHR43585:SF2; ATP-GRASP ENZYME FSQD; 1.
DR PANTHER; PTHR43585; FUMIPYRROLE BIOSYNTHESIS PROTEIN C; 1.
DR Pfam; PF13535; ATP-grasp_4; 1.
DR SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR PROSITE; PS50975; ATP_GRASP; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU00409}; Ligase {ECO:0000256|ARBA:ARBA00022598};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00409}.
FT DOMAIN 120..314
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
SQ SEQUENCE 403 AA; 45926 MW; 438ABA301BDF0B91 CRC64;
MEQKTIVCIS CYYKGYDFME EMQNLGNRVI LITSENLKEK NWPWHAINEV FYMPEIKPSV
WDLEHLVQGF SHLMKTRKVD AVIALDDYDV EKAALVRETF RIPGMGQTTH RYFRDKLAMR
QKAKNSGINV PEFTAVFNDA EVAEFAKNVP APWVLKPRSE ASASGIKKLK SQEELWQALE
NLGDERHLFL LESFKPGDVY HVDSLTFNAK TIFTSSSKYL APPMQVSHEG GVFRTRTLGR
STAEFKALEK ANVQVLSNFG LQNGATHTEF IRGKEDGKWY FLETSSRVGG AHIPDLVEAS
SGINIWREWA KIEDALLKGL DYSISKPTGY YAGLIIALIK EKHPDYKYFE SEETVKFLPI
DYHIGIVYKS SKSDLVQTRL DETAVKIHED MLSIIPPKDK PTS
//
