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Database: UniProt
Entry: A0A0C2G9C4_9ACTN
LinkDB: A0A0C2G9C4_9ACTN
Original site: A0A0C2G9C4_9ACTN 
ID   A0A0C2G9C4_9ACTN        Unreviewed;       211 AA.
AC   A0A0C2G9C4;
DT   01-APR-2015, integrated into UniProtKB/TrEMBL.
DT   01-APR-2015, sequence version 1.
DT   27-MAR-2024, entry version 34.
DE   SubName: Full=ATP-binding protein {ECO:0000313|EMBL:KII00054.1};
GN   ORFNames=LP52_03710 {ECO:0000313|EMBL:KII00054.1};
OS   Streptomonospora alba.
OC   Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC   Nocardiopsaceae; Streptomonospora.
OX   NCBI_TaxID=183763 {ECO:0000313|EMBL:KII00054.1, ECO:0000313|Proteomes:UP000031675};
RN   [1] {ECO:0000313|Proteomes:UP000031675}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YIM 90003 {ECO:0000313|Proteomes:UP000031675};
RX   PubMed=25601074; DOI=10.1016/j.chembiol.2014.11.017;
RA   Metelev M., Tietz J.I., Melby J.O., Blair P.M., Zhu L., Livnat I.,
RA   Severinov K., Mitchell D.A.;
RT   "Structure, bioactivity, and resistance mechanism of streptomonomicin, an
RT   unusual lasso Peptide from an understudied halophilic actinomycete.";
RL   Chem. Biol. 22:241-250(2015).
CC   -!- SIMILARITY: Belongs to the GPN-loop GTPase family.
CC       {ECO:0000256|ARBA:ARBA00005290}.
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:KII00054.1}.
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DR   EMBL; JROO01000006; KII00054.1; -; Genomic_DNA.
DR   RefSeq; WP_040270733.1; NZ_JROO01000006.1.
DR   AlphaFoldDB; A0A0C2G9C4; -.
DR   STRING; 183763.LP52_03710; -.
DR   OrthoDB; 4303541at2; -.
DR   Proteomes; UP000031675; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   CDD; cd00882; Ras_like_GTPase; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   InterPro; IPR004130; Gpn.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR42708; ATP/GTP-BINDING PROTEIN-RELATED; 1.
DR   PANTHER; PTHR42708:SF1; GLIDING MOTILITY PROTEIN MGLA; 1.
DR   Pfam; PF03029; ATP_bind_1; 1.
DR   PRINTS; PR00449; RASTRNSFRMNG.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000313|EMBL:KII00054.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000031675}.
FT   REGION          1..21
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   211 AA;  22652 MW;  2857166CD8AF3EF7 CRC64;
     MHSNASDIPV QSPGSPAPAP LSADAQDALK IVVVGGFGVG KTTMVGAVSE IRPLSTEEVM
     TEASVGVDDP SRVRSKTTTT AAFDFGRITI TEDKILYLFG APGQERFWFL WDQLFAGSLG
     AVVLVDPRRV EESWYAIDRL EAHGTPFVVA INRFEAGPGL DALREALDLS EGVPLVECDA
     RSRDDCKAVL ISLVRHLNDL YAPSPAREGT P
//
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