ID A0A2P2BTG1_9FIRM Unreviewed; 1184 AA.
AC A0A2P2BTG1;
DT 23-MAY-2018, integrated into UniProtKB/TrEMBL.
DT 23-MAY-2018, 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=FRIFI_2127 {ECO:0000313|EMBL:CEI73655.1};
OS Romboutsia hominis.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Peptostreptococcaceae;
OC Romboutsia.
OX NCBI_TaxID=1507512 {ECO:0000313|EMBL:CEI73655.1, ECO:0000313|Proteomes:UP000245695};
RN [1] {ECO:0000313|EMBL:CEI73655.1, ECO:0000313|Proteomes:UP000245695}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FRIFI {ECO:0000313|EMBL:CEI73655.1,
RC ECO:0000313|Proteomes:UP000245695};
RA Hornung B.V.;
RL Submitted (SEP-2014) 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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LN650648; CEI73655.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2P2BTG1; -.
DR Proteomes; UP000245695; Chromosome Chromosome1.
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; 1.
DR Gene3D; 1.20.1060.20; -; 1.
DR Gene3D; 3.30.70.1620; -; 1.
DR Gene3D; 6.10.140.1720; -; 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; 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:UP000245695}.
FT DOMAIN 520..636
FT /note="SMC hinge"
FT /evidence="ECO:0000259|SMART:SM00968"
FT COILED 167..201
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 227..366
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 395..468
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 670..795
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 824..921
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 962..1031
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 1184 AA; 136324 MW; 1615F7DFEF087B95 CRC64;
MYLKRLELKG FKSFPTKTDI LFNQGITAIV GPNGSGKSNI SDAVRWVLGE QSIKSLRGDK
LEDVIFAGTD TKKAMSYCEV SLTIDNSEDK LNIDFSEITI KRRAYRSGES EFFLNNKPCR
LKDIKELLLD TGIGKDGYSI IEQGKVDEIL SNNPVNRRKV FDEACGISKF RYKKQEAERN
LKNTKENLER IEDIYIEIEN QLKPLFSQQE KAKKYIELND KLKTIEVNSY IKEIDLLEKD
LNEALKHSKL LEEQAIETNN QKVKLENNLN ETSKEVEDIS ENINKSIDYI NSIKSVISQK
DAQLNLINEK IKNLNESILK SENELSEIGN KISSNENLIK DLEINKIEKE NTIKSLTEDI
DLLDKNNLSK KESIEKVNSK IEGLKDGIIN LLNKKQESSN RLSTLSANME NINSRDKSID
LEISEVKSDL NEKFTELNDI KLNVSQKNAE LEKLKLKELE NKNTLEELIN HSKKLEKQIQ
DGNYSINNYN SKLNIYIDME NHNEGFNKGV KEVLKNKSLK GIHGALGQVI TTSEKYEKAI
ESALGAYLQN IITSDENSAK IAINYLKKNN LGRVTFLPLN TIKANKINPS TIKSNTKFIG
IASDLLSYDE KYKNIIENIL GRTIIIDNID EGIKFARETG HRYKVVTLDG EILNPGGSLT
GGSFKNNTSI LSRKRLINEY SQKLEDAKKE TKEFIKQKQE KDNNISTKKN DILKIEEEVK
ELEKNIIIES SKLNRVEEEI KNINISINKL QNEKDGLISN LKYTKDKLDI VKIEIEKMDK
EHEENKETIE KLSLELKKSN DYYEKDREKH DNLNLKLVKD KQVLESIYAD IKRIKNENEE
LRLKKGNIEK SIENQNIEIS KLREETVIEE TEKVSLNKQL SDNSRNLENR KLAKEDLKQK
LEEHNKNLKI IDRQYIDLKE SLFKVESKID RIKVSKEDYI NNLFEKYELT VADAMNIKDT
SIEIDKKKLE SLKREIRNLG NVNIDAIKEY EEVKERYDFY SEQKQDLEQS IEAIENLIEE
LESNMKTEFK VKFNEINDNF KMVYKRLFGG GRGELIILDE KDILESDIEI VAQPPGKKMK
NLNLLSGGEK ALTAISILFS ILLAKPTPFC ILDEIEAPLD DANIFRFGEF LKELSQDTQF
ISVTHRRGTM EASDYIYGVT MQEKAISKVL SLKLNEAEKM TDII
//