ID   RFCS_METBF              Reviewed;         334 AA.
AC   Q46C63;
DT   11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2005, sequence version 1.
DT   03-AUG-2022, entry version 97.
DE   RecName: Full=Replication factor C small subunit {ECO:0000255|HAMAP-Rule:MF_01509};
DE            Short=RFC small subunit {ECO:0000255|HAMAP-Rule:MF_01509};
DE   AltName: Full=Clamp loader small subunit {ECO:0000255|HAMAP-Rule:MF_01509};
GN   Name=rfcS {ECO:0000255|HAMAP-Rule:MF_01509}; OrderedLocusNames=Mbar_A1582;
OS   Methanosarcina barkeri (strain Fusaro / DSM 804).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanosarcinales; Methanosarcinaceae; Methanosarcina.
OX   NCBI_TaxID=269797;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Fusaro / DSM 804;
RX   PubMed=16980466; DOI=10.1128/jb.00810-06;
RA   Maeder D.L., Anderson I., Brettin T.S., Bruce D.C., Gilna P., Han C.S.,
RA   Lapidus A., Metcalf W.W., Saunders E., Tapia R., Sowers K.R.;
RT   "The Methanosarcina barkeri genome: comparative analysis with
RT   Methanosarcina acetivorans and Methanosarcina mazei reveals extensive
RT   rearrangement within methanosarcinal genomes.";
RL   J. Bacteriol. 188:7922-7931(2006).
CC   -!- FUNCTION: Part of the RFC clamp loader complex which loads the PCNA
CC       sliding clamp onto DNA. {ECO:0000255|HAMAP-Rule:MF_01509}.
CC   -!- SUBUNIT: Heteromultimer composed of small subunits (RfcS) and large
CC       subunits (RfcL). {ECO:0000255|HAMAP-Rule:MF_01509}.
CC   -!- SIMILARITY: Belongs to the activator 1 small subunits family. RfcS
CC       subfamily. {ECO:0000255|HAMAP-Rule:MF_01509}.
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DR   EMBL; CP000099; AAZ70529.1; -; Genomic_DNA.
DR   RefSeq; WP_011306575.1; NC_007355.1.
DR   AlphaFoldDB; Q46C63; -.
DR   SMR; Q46C63; -.
DR   STRING; 269797.Mbar_A1582; -.
DR   PRIDE; Q46C63; -.
DR   EnsemblBacteria; AAZ70529; AAZ70529; Mbar_A1582.
DR   GeneID; 3625358; -.
DR   KEGG; mba:Mbar_A1582; -.
DR   eggNOG; arCOG00469; Archaea.
DR   HOGENOM; CLU_042324_1_0_2; -.
DR   OMA; SCNYSSQ; -.
DR   OrthoDB; 37207at2157; -.
DR   GO; GO:0005663; C:DNA replication factor C complex; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0003689; F:DNA clamp loader activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006260; P:DNA replication; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.40.50.300; -; 1.
DR   HAMAP; MF_01509; RfcS; 1.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR003959; ATPase_AAA_core.
DR   InterPro; IPR008921; DNA_pol3_clamp-load_cplx_C.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR023748; Rep_factor-C_ssu_arc.
DR   InterPro; IPR013748; Rep_factorC_C.
DR   Pfam; PF00004; AAA; 1.
DR   Pfam; PF08542; Rep_fac_C; 1.
DR   SMART; SM00382; AAA; 1.
DR   SUPFAM; SSF48019; SSF48019; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
PE   3: Inferred from homology;
KW   ATP-binding; DNA replication; Nucleotide-binding.
FT   CHAIN           1..334
FT                   /note="Replication factor C small subunit"
FT                   /id="PRO_0000245639"
FT   BINDING         49..56
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01509"
SQ   SEQUENCE   334 AA;  37811 MW;  88F7938915E6D14D CRC64;
     MEDSTIKEEI WIEKYRPVRL DQVAGQEETI ERLKSYVATK NLPHLLFSGP PGVGKTASAV
     SIAREIFGED LWRENFTELN ASDERGIDVV RTKIKNFAKT APMGGAEFKI IFLDEADALT
     SDAQSALRRT MERFSNNCRF ILSCNYSSRI IEPIQSRCAV FRFRRLSDEA IRKRLEYIAK
     DQVLSITEDG YEALVYVSQG DMRKAVNSLQ AAAFVEPNKS ISRGTIYRTT ATANPEDIRN
     LIETALRGNF RVARKELNRL LYEEGLSGED IVGQIYRAIS EMDNRMILDL GLSEKRIVEL
     VDIIGEIDFR LTEGATEKIQ LEALLAHFAL SNPD