ID U2JW21_9FIRM Unreviewed; 1194 AA.
AC U2JW21;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2013, sequence version 1.
DT 24-JAN-2024, entry version 42.
DE RecName: Full=Chromosome partition protein Smc {ECO:0000256|HAMAP-Rule:MF_01894};
GN Name=smc {ECO:0000256|HAMAP-Rule:MF_01894};
GN ORFNames=HMPREF1987_00699 {ECO:0000313|EMBL:ERJ84227.1};
OS Peptostreptococcaceae bacterium oral taxon 113 str. W5053.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Peptostreptococcaceae.
OX NCBI_TaxID=1321784 {ECO:0000313|EMBL:ERJ84227.1, ECO:0000313|Proteomes:UP000016618};
RN [1] {ECO:0000313|EMBL:ERJ84227.1, ECO:0000313|Proteomes:UP000016618}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=W5053 {ECO:0000313|EMBL:ERJ84227.1,
RC ECO:0000313|Proteomes:UP000016618};
RA Weinstock G., Sodergren E., Wylie T., Fulton L., Fulton R., Fronick C.,
RA O'Laughlin M., Godfrey J., Miner T., Herter B., Appelbaum E., Cordes M.,
RA Lek S., Wollam A., Pepin K.H., Palsikar V.B., Mitreva M., Wilson R.K.;
RL Submitted (AUG-2013) 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 -!- 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:ERJ84227.1}.
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DR EMBL; AWVB01000025; ERJ84227.1; -; Genomic_DNA.
DR AlphaFoldDB; U2JW21; -.
DR STRING; 1321784.HMPREF1987_00699; -.
DR PATRIC; fig|1321784.3.peg.659; -.
DR eggNOG; COG1196; Bacteria.
DR HOGENOM; CLU_001042_2_2_9; -.
DR OrthoDB; 9808768at2; -.
DR Proteomes; UP000016618; 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; 1.
DR Gene3D; 1.20.1060.20; -; 1.
DR Gene3D; 3.30.70.1620; -; 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:UP000016618}.
FT DOMAIN 532..642
FT /note="SMC hinge"
FT /evidence="ECO:0000259|SMART:SM00968"
FT COILED 178..208
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 255..408
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 444..485
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 853..894
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 993..1027
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT BINDING 39..46
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
SQ SEQUENCE 1194 AA; 138519 MW; 542E29852D207D99 CRC64;
MDYGEINMKL KSIEIYGFKS FAEPIQLNFN QPVSIIVGPN GSGKSNISDA VWWVLGEQSA
KNLRGGTMQD IIFAGTEKKQ ALNYARVTIT FDNETGDIPL EYKEISITRK LFRNGESEYY
INKSQVRLKD IRELFMDTGI GKEGYSLIGQ GKIDEIISGN SDVRREIFEE ASGVTKYKYK
LENSIRKLEK TKDDIQRIED ILFQLNERYD YLKTEAEKAQ KGIEASKELE ELELENYYCH
IMQMKNNLHD KKSTTELMKE QVNELEKLLK IKKQDLSPLK NEKDNLKKKK DILLSSCNEM
SQESIVADKR ILVLTEKENY LQTELKRLQR ESEEFSIRME NLEKNLSEKK ESFIKLIQKV
NIIRLEKEEI EKYKDNYIIQ VNEIEKQIKQ QENKISKGTE KLNDLIVRQT TRHEITQNIL
NNQIQIKQEQ DKIEKSLAQI GIEIENIQES AEIEIEKANR LKQHIEEIKR RIIKTEEVAH
SLQIEISKTE ALSQEKRSNY SILDNMYKNY EGYYYSVQQL MQESKKRKEV KELFLGVLGD
LIHTDIKYQR AIDAALGSAV QNIIVKDEDA AKTIIDYLKK NKIGRMTFLP ISKIKGKKIS
WNLEGVVASS VVQFDNQIKE IVESFLGRTI LVGNMDLAIR LRNSDKQNLR FITLDGEVFN
PIGSIIGGYS KSGKSSLINR KHSLDILKKE LEDIEHKLVE KRRSFEETGK KIKLEKEKLS
DLTDALRNIN VSIENRKKEE DTLNLKYALL SDNLLQLKKK WEEKKIEPEK DLLQDVDNQK
DIIQKDKEFL NLLEEKNLEI KVKSDETLKR FYQKVNELEI GNRDISLLKN DIGSLEDSIQ
TLFQSHTNSM QLMKKLIEDN KILENDLIKS KSEKDELEKS LNIARTELEG NQKKCNEIEE
IIVQKTNESE KINNDLLDIR HRMEISAIQV SGYEEKLEEL TVELFSAYSY SVEDLEKIFS
GKSPSTVSKA KLKSIRDTVK EIGYFSIASI HEFQEVLKEK EFTEIQLNDL NQSKEDITEI
ITDLENRIIF QFEKETSQIK LRFQEVFHSL FGGGQAELVI EEVCSLKPII EIKAQPPGKN
LQNLSLLSGG EKTLTAIALL FAIFSIRPTP FCILDEIDAS LDETNIGRYV DYLTEFHKEI
QFIVITHRKR TMEMADQLYG VTMDDDGISK VLSLELSERE NDLYVEESRG YDYD
//
