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Database: UniProt
Entry: C5NY10_9BACL
LinkDB: C5NY10_9BACL
Original site: C5NY10_9BACL 
ID   C5NY10_9BACL            Unreviewed;       411 AA.
AC   C5NY10;
DT   01-SEP-2009, integrated into UniProtKB/TrEMBL.
DT   01-SEP-2009, sequence version 1.
DT   27-MAR-2024, entry version 40.
DE   RecName: Full=ATP-grasp domain-containing protein {ECO:0000259|PROSITE:PS50975};
GN   ORFNames=GEMHA0001_0345 {ECO:0000313|EMBL:EER67739.1};
OS   Gemella haemolysans ATCC 10379.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Gemellaceae; Gemella.
OX   NCBI_TaxID=546270 {ECO:0000313|EMBL:EER67739.1, ECO:0000313|Proteomes:UP000006004};
RN   [1] {ECO:0000313|EMBL:EER67739.1, ECO:0000313|Proteomes:UP000006004}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 10379 {ECO:0000313|EMBL:EER67739.1,
RC   ECO:0000313|Proteomes:UP000006004};
RA   Fulton L., Clifton S., Chinwalla A.T., Mitreva M., Sodergren E.,
RA   Weinstock G., Clifton S., Dooling D.J., Fulton B., Minx P., Pepin K.H.,
RA   Johnson M., Bhonagiri V., Nash W.E., Mardis E.R., Wilson R.K.;
RL   Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:EER67739.1, ECO:0000313|Proteomes:UP000006004}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 10379 {ECO:0000313|EMBL:EER67739.1,
RC   ECO:0000313|Proteomes:UP000006004};
RA   Sebastian Y., Madupu R., Durkin A.S., Torralba M., Methe B., Sutton G.G.,
RA   Strausberg R.L., Nelson K.E.;
RL   Submitted (JUN-2009) 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:EER67739.1}.
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DR   EMBL; ACDZ02000014; EER67739.1; -; Genomic_DNA.
DR   AlphaFoldDB; C5NY10; -.
DR   eggNOG; COG1181; Bacteria.
DR   Proteomes; UP000006004; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
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          140..331
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS50975"
SQ   SEQUENCE   411 AA;  48145 MW;  0E61EDE93AF8C1FD CRC64;
     MFHWKISEVY GKLMNKIRKE GIIMNYLLVS PNFPTSQESF ARKLVEKGVK VLGIGSESYD
     NLTDGLKNSL TEYYKVNDLE NYEEVLRGVA FLIYKHGVID RVESNNEHWL MLDSIIREQF
     NITGVKPKKL DFTKYKSKMK ERFIKAKVPV AKGRAVKNIR ELEKAIKDIK LPVIAKPNNG
     VGANNTFKLI SKEDVEDFKN QWDQEVVYFI ESYIDNGVLC TYDGLIDSKG EVVFETSFYY
     TKPTLDLLND SLDYGNIISR EIDPKLKEYG RNIVKEFGMK ERFFHIEFFK LPNNDYIALE
     YNNRIAGGYT VDLYNHTYEC DLFEMYADVV VGNSPKKVKN NYNGVALSRR DKYTYKYTNE
     DIYNRYSKEL RLIDRVPEVF ATAMGEWMYI LVDENMENIS EMMTYIHEKN E
//
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