ID A0A1G4P4C2_9FIRM Unreviewed; 1185 AA.
AC A0A1G4P4C2;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE RecName: Full=Chromosome partition protein Smc {ECO:0000256|HAMAP-Rule:MF_01894};
GN Name=smc {ECO:0000256|HAMAP-Rule:MF_01894};
GN ORFNames=SAMN02910456_00191 {ECO:0000313|EMBL:SCW27077.1};
OS Ruminococcaceae bacterium YRB3002.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae.
OX NCBI_TaxID=1520819 {ECO:0000313|EMBL:SCW27077.1, ECO:0000313|Proteomes:UP000199293};
RN [1] {ECO:0000313|EMBL:SCW27077.1, ECO:0000313|Proteomes:UP000199293}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YRB3002 {ECO:0000313|EMBL:SCW27077.1,
RC ECO:0000313|Proteomes:UP000199293};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Required for chromosome condensation and partitioning.
CC {ECO:0000256|HAMAP-Rule:MF_01894}.
CC -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_01894}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01894}.
CC -!- DOMAIN: Contains large globular domains required for ATP hydrolysis at
CC each terminus and a third globular domain forming a flexible hinge near
CC the middle of the molecule. These domains are separated by coiled-coil
CC structures. {ECO:0000256|HAMAP-Rule:MF_01894}.
CC -!- SIMILARITY: Belongs to the SMC family. SMC3 subfamily.
CC {ECO:0000256|ARBA:ARBA00005917}.
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DR EMBL; FMTG01000002; SCW27077.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G4P4C2; -.
DR STRING; 1520819.SAMN02910456_00191; -.
DR OrthoDB; 9808768at2; -.
DR Proteomes; UP000199293; Unassembled WGS sequence.
DR GO; GO:0005694; C:chromosome; IEA:InterPro.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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:UniProtKB-UniRule.
DR GO; GO:0030261; P:chromosome condensation; IEA:InterPro.
DR GO; GO:0007059; P:chromosome segregation; IEA:UniProtKB-UniRule.
DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-UniRule.
DR GO; GO:0007062; P:sister chromatid cohesion; IEA:InterPro.
DR CDD; cd03278; ABC_SMC_barmotin; 2.
DR Gene3D; 1.10.287.1490; -; 1.
DR Gene3D; 1.20.1060.20; -; 1.
DR Gene3D; 3.30.70.1620; -; 1.
DR Gene3D; 6.10.140.1720; -; 1.
DR Gene3D; 1.10.287.950; Methyl-accepting chemotaxis protein; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR HAMAP; MF_01894; Smc_prok; 1.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR003395; RecF/RecN/SMC_N.
DR InterPro; IPR024704; SMC.
DR InterPro; IPR010935; SMC_hinge.
DR InterPro; IPR036277; SMC_hinge_sf.
DR InterPro; IPR011890; SMC_prok.
DR NCBIfam; TIGR02168; SMC_prok_B; 1.
DR PANTHER; PTHR43977; STRUCTURAL MAINTENANCE OF CHROMOSOMES PROTEIN 3; 1.
DR PANTHER; PTHR43977:SF1; STRUCTURAL MAINTENANCE OF CHROMOSOMES PROTEIN 3; 1.
DR Pfam; PF06470; SMC_hinge; 1.
DR Pfam; PF02463; SMC_N; 1.
DR PIRSF; PIRSF005719; SMC; 1.
DR SMART; SM00968; SMC_hinge; 1.
DR SUPFAM; SSF58104; Methyl-accepting chemotaxis protein (MCP) signaling domain; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF75553; Smc hinge domain; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|HAMAP-Rule:MF_01894};
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|HAMAP-
KW Rule:MF_01894};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_01894};
KW DNA-binding {ECO:0000256|HAMAP-Rule:MF_01894};
KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01894};
KW Reference proteome {ECO:0000313|Proteomes:UP000199293}.
FT DOMAIN 525..644
FT /note="SMC hinge"
FT /evidence="ECO:0000259|SMART:SM00968"
FT COILED 167..201
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 248..296
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 346..429
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 686..944
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 1011..1038
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT BINDING 32..39
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
SQ SEQUENCE 1185 AA; 135325 MW; CC385CA8ED27424E CRC64;
MYLKRIEIQG FKSFPESTLI EFDSGMTAIV GPNGSGKSNV TDAVRWVLGE QSAKSLRGGK
MEDVIFNGTS TRKAMNYAEV TLTLDNIDRY IDYDFPEIQI TRRLYRSGES EYQINKVNCR
LKDIVGLFLD TGIGKDGYSI VGQGRVDEIL STKSEDRRYV IEEAAGIVKY KVRKDEAERK
LNQTEQNLLR IDDVLAELNE RFGPLEEQSK KAIRYHRVYE SMRSKDISLL VHKITTAQEA
MGDSAGIREQ LEREIKKQED RFVALREENR EMSEKSETLE DTIEEKRQEL SDVTEEQHEN
NSNRKVLAER MNSINKEIND ASYDNDAATA RIKVLEGERK AHLDHAEEIL GECNELKKAS
EALNRRREEI LKEYEKEEKS ISAIRARIEG KTKDLNESRE NIKTVAARIE ALGEQITRLS
DQLNNIRSSG EELKASLEEA DKHWKEMTKT EGEVQDDIRT RDDKLKALSE KMKELNDFFE
KNNSEFLSLC ARLRTLKDLE KRKEGYQESV RRLMDEAEHD KNLKSKMVGV LGDLISVDRK
YETAIEIALG SAIHNVVTDL ESEAADLIEV LKTKRLGRVT FLPIENIEAR PMPSDILKKA
SGQKGYIDVA SELIKCDVML NDIVSNLLGR IIIADNLDNA RKIASSVRHQ VKIITLDGDS
VNPGGSLTGG SVRKSGVGIL GRAREIEDLT KKTEDLEAKL SDNEENRQEL DDVAGTLKKE
IMLLGEQLKY YSMERVKAES EYRNIEDKIK ENDDRQRETE ELLKKISTEK LRLEDDLEEL
GRIEQELGNE LFSFTEDSKS GDEKVQEFSE RLDGIKDEMA DITSKSERLL AERNGVIKLA
DHIKEQIDAI NREIDERREQ IADAEKQIEE ITKEINGITE TLAKLEVSQR EYEKEIQELT
RQKAEIDSSM SGFVSNLTSI NDSINNLRNK LNTHISKYDK YITEIDAAKS RLWEDYEVTY
DNIRDEALPV EDVTALAKEI SSLKSEIRNI GPVNPDSVEE FRELSERLEF MTAQRNDIAK
AKEDLEKVIS DLLNEMRQQF ITQFEIINNN FKRVFFDLFG GGTAEIVLDS DDVLECNIEI
KAQPPGKRLQ SLTLLSGGER CLTAIALLFA ILELKPSPFV ILDEVEAALD DVNVSRFTDF
VRRYCVKSQF ILVTHRKGTM EACDRMYGVT MAERGISKIL SMRFS
//
