ID K5DAT9_RHOBT Unreviewed; 387 AA.
AC K5DAT9;
DT 09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT 09-JAN-2013, sequence version 1.
DT 27-MAR-2024, entry version 47.
DE SubName: Full=Ribosomal protein S6 modification protein {ECO:0000313|EMBL:EKJ99567.1};
GN ORFNames=RBSH_05129 {ECO:0000313|EMBL:EKJ99567.1};
OS Rhodopirellula baltica SH28.
OC Bacteria; Planctomycetota; Planctomycetia; Pirellulales; Pirellulaceae;
OC Rhodopirellula.
OX NCBI_TaxID=993517 {ECO:0000313|EMBL:EKJ99567.1, ECO:0000313|Proteomes:UP000007993};
RN [1] {ECO:0000313|EMBL:EKJ99567.1, ECO:0000313|Proteomes:UP000007993}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SH28 {ECO:0000313|EMBL:EKJ99567.1,
RC ECO:0000313|Proteomes:UP000007993};
RX PubMed=23273849;
RA Wegner C.E., Richter-Heitmann T., Klindworth A., Klockow C., Richter M.,
RA Achstetter T., Glockner F.O., Harder J.;
RT "Expression of sulfatases in Rhodopirellula baltica and the diversity of
RT sulfatases in the genus Rhodopirellula.";
RL Mar. Genomics 0:0-0(2012).
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:EKJ99567.1}.
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DR EMBL; AMCW01000142; EKJ99567.1; -; Genomic_DNA.
DR AlphaFoldDB; K5DAT9; -.
DR PATRIC; fig|993517.3.peg.5558; -.
DR Proteomes; UP000007993; 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 GO; GO:0008324; F:monoatomic cation transmembrane transporter activity; IEA:InterPro.
DR GO; GO:0006813; P:potassium ion transport; IEA:InterPro.
DR GO; GO:0036211; P:protein modification process; IEA:InterPro.
DR GO; GO:0006412; P:translation; IEA:UniProtKB-KW.
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 Gene3D; 3.30.70.1450; Regulator of K+ conductance, C-terminal domain; 1.
DR InterPro; IPR011761; ATP-grasp.
DR InterPro; IPR013651; ATP-grasp_RimK-type.
DR InterPro; IPR013815; ATP_grasp_subdomain_1.
DR InterPro; IPR006037; RCK_C.
DR InterPro; IPR036721; RCK_C_sf.
DR InterPro; IPR041107; Rimk_N.
DR InterPro; IPR004666; Rp_bS6_RimK/Lys_biosynth_LsyX.
DR NCBIfam; TIGR00768; rimK_fam; 1.
DR PANTHER; PTHR21621:SF0; BETA-CITRYLGLUTAMATE SYNTHASE B-RELATED; 1.
DR PANTHER; PTHR21621; RIBOSOMAL PROTEIN S6 MODIFICATION PROTEIN; 1.
DR Pfam; PF08443; RimK; 1.
DR Pfam; PF18030; Rimk_N; 1.
DR Pfam; PF02080; TrkA_C; 1.
DR SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR SUPFAM; SSF116726; TrkA C-terminal domain-like; 1.
DR PROSITE; PS50975; ATP_GRASP; 1.
DR PROSITE; PS51202; RCK_C; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|PROSITE-ProRule:PRU00409};
KW Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00409};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917}.
FT DOMAIN 86..269
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 278..362
FT /note="RCK C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51202"
FT REGION 361..387
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 370..387
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 387 AA; 42528 MW; 9A6903FB31DA3D0F CRC64;
MEAAEQRGIK AKVLNTLKFA IDLAEGEPDL YYRSKQLSDY DGVLPRIGAS ITYFGTAVVR
QFEQMDVFCA NSSAGISNSR DKLRSLQILS RHQIGIPKTT FVRDRKDILP AIERVGGSPV
IIKLLEGTQG VGVILAENVK VAEAIIETLQ STKQNVLVQQ FVAESRGKDI RAFVIGDRVV
AAMRRVAVGN EFRSNVHRGG QTEAVVLDET YAETAVRAAQ IMGLRVAGVD MLEGTNGPQV
MEVNSSPGLE GIESATKLDI AGAIIDYMSA QVDFPEVDVR QRLTVSRGYG VTELHVRDGS
DYVGKTIDES GLPELDINVL TLYRGTTVIP NPRLKRTLEP HDRLLCFGKL EAMRGMVPEK
VRKQRRPKIK RLPDSAATIH AESSRDD
//
