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Database: UniProt
Entry: C7MLK1_CRYCD
LinkDB: C7MLK1_CRYCD
Original site: C7MLK1_CRYCD 
ID   C7MLK1_CRYCD            Unreviewed;       355 AA.
AC   C7MLK1;
DT   13-OCT-2009, integrated into UniProtKB/TrEMBL.
DT   13-OCT-2009, sequence version 1.
DT   27-MAR-2024, entry version 85.
DE   RecName: Full=Small ribosomal subunit biogenesis GTPase RsgA {ECO:0000256|HAMAP-Rule:MF_01820};
DE            EC=3.6.1.- {ECO:0000256|HAMAP-Rule:MF_01820};
GN   Name=rsgA {ECO:0000256|HAMAP-Rule:MF_01820};
GN   OrderedLocusNames=Ccur_00740 {ECO:0000313|EMBL:ACU93807.1};
OS   Cryptobacterium curtum (strain ATCC 700683 / DSM 15641 / CCUG 43107 /
OS   12-3).
OC   Bacteria; Actinomycetota; Coriobacteriia; Eggerthellales; Eggerthellaceae;
OC   Cryptobacterium.
OX   NCBI_TaxID=469378 {ECO:0000313|EMBL:ACU93807.1, ECO:0000313|Proteomes:UP000000954};
RN   [1] {ECO:0000313|EMBL:ACU93807.1, ECO:0000313|Proteomes:UP000000954}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700683 / DSM 15641 / 12-3
RC   {ECO:0000313|Proteomes:UP000000954};
RX   PubMed=21304644; DOI=10.40456/sigs.12260;
RA   Mavrommatis K., Pukall R., Rohde C., Chen F., Sims D., Brettin T.,
RA   Kuske C., Detter J.C., Han C., Lapidus A., Copeland A., Glavina Del Rio T.,
RA   Nolan M., Lucas S., Tice H., Cheng J.F., Bruce D., Goodwin L., Pitluck S.,
RA   Ovchinnikova G., Pati A., Ivanova N., Chen A., Palaniappan K., Chain P.,
RA   D'haeseleer P., Goker M., Bristow J., Eisen J.A., Markowitz V.,
RA   Hugenholtz P., Rohde M., Klenk H.P., Kyrpides N.C.;
RT   "Complete genome sequence of Cryptobacterium curtum type strain (12-3).";
RL   Stand. Genomic Sci. 1:93-100(2009).
CC   -!- FUNCTION: One of several proteins that assist in the late maturation
CC       steps of the functional core of the 30S ribosomal subunit. Helps
CC       release RbfA from mature subunits. May play a role in the assembly of
CC       ribosomal proteins into the subunit. Circularly permuted GTPase that
CC       catalyzes slow GTP hydrolysis, GTPase activity is stimulated by the 30S
CC       ribosomal subunit. {ECO:0000256|HAMAP-Rule:MF_01820}.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_01820};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000256|HAMAP-Rule:MF_01820};
CC   -!- SUBUNIT: Monomer. Associates with 30S ribosomal subunit, binds 16S
CC       rRNA. {ECO:0000256|HAMAP-Rule:MF_01820}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01820}.
CC   -!- SIMILARITY: Belongs to the TRAFAC class YlqF/YawG GTPase family. RsgA
CC       subfamily. {ECO:0000256|HAMAP-Rule:MF_01820}.
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DR   EMBL; CP001682; ACU93807.1; -; Genomic_DNA.
DR   AlphaFoldDB; C7MLK1; -.
DR   STRING; 469378.Ccur_00740; -.
DR   KEGG; ccu:Ccur_00740; -.
DR   eggNOG; COG1162; Bacteria.
DR   HOGENOM; CLU_033617_0_1_11; -.
DR   Proteomes; UP000000954; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0042274; P:ribosomal small subunit biogenesis; IEA:UniProtKB-UniRule.
DR   CDD; cd01854; YjeQ_EngC; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   HAMAP; MF_01820; GTPase_RsgA; 1.
DR   InterPro; IPR030378; G_CP_dom.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR004881; Ribosome_biogen_GTPase_RsgA.
DR   InterPro; IPR010914; RsgA_GTPase_dom.
DR   NCBIfam; TIGR00157; ribosome small subunit-dependent GTPase A; 1.
DR   PANTHER; PTHR32120; SMALL RIBOSOMAL SUBUNIT BIOGENESIS GTPASE RSGA; 1.
DR   PANTHER; PTHR32120:SF10; SMALL RIBOSOMAL SUBUNIT BIOGENESIS GTPASE RSGA; 1.
DR   Pfam; PF03193; RsgA_GTPase; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS50936; ENGC_GTPASE; 1.
DR   PROSITE; PS51721; G_CP; 1.
PE   3: Inferred from homology;
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01820};
KW   GTP-binding {ECO:0000256|HAMAP-Rule:MF_01820};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_01820};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_01820};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_01820}; Reference proteome {ECO:0000313|Proteomes:UP000000954};
KW   Ribosome biogenesis {ECO:0000256|HAMAP-Rule:MF_01820};
KW   RNA-binding {ECO:0000256|HAMAP-Rule:MF_01820};
KW   rRNA-binding {ECO:0000256|HAMAP-Rule:MF_01820};
KW   Zinc {ECO:0000256|HAMAP-Rule:MF_01820}.
FT   DOMAIN          77..238
FT                   /note="CP-type G"
FT                   /evidence="ECO:0000259|PROSITE:PS51721"
FT   DOMAIN          86..236
FT                   /note="EngC GTPase"
FT                   /evidence="ECO:0000259|PROSITE:PS50936"
FT   REGION          300..355
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         124..127
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01820"
FT   BINDING         180..188
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01820"
FT   BINDING         261
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01820"
FT   BINDING         266
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01820"
FT   BINDING         268
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01820"
FT   BINDING         274
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01820"
SQ   SEQUENCE   355 AA;  38033 MW;  EB97423F725416B7 CRC64;
     MILKAQVVQL DRGFPLVRLA SGDLIRCKHA TSLVKEATQR AVIGDWVKIE TDDAADKAQI
     VEILPRQQVL LRKDPAERSM VQVLAANFDT VIIAHPLPGL NIRRLERELV VACDTGARVV
     VALTKSDLVE SDQVRTDAVA AVQAVVAPGI GVIEVSTVNQ IGIDAVRALV STGTQAVLMG
     RSGAGKSSLI NALADQEVQA TQPVRAADGK GRHTTVNRTM VRIQGGGEVI DMPGVRGLGL
     WDAQAGIDAA FPDVVEAARN CRFRDCRHQG DAGCGVGAAI KAGNITPERV AAYVRLSEEN
     SQQLKRNKEA QWQTGAGRSG RSRQPYSRDV ARSSNARKNS YKTARNSNAR NSNAQ
//
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