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Database: UniProt
Entry: A0A2P2BTG1_9FIRM
LinkDB: A0A2P2BTG1_9FIRM
Original site: A0A2P2BTG1_9FIRM 
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}.
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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
//
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