ID F4LPD0_TREBD Unreviewed; 977 AA.
AC F4LPD0;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 27-MAR-2024, entry version 64.
DE RecName: Full=Chromosome partition protein Smc {ECO:0000256|HAMAP-Rule:MF_01894};
GN Name=smc {ECO:0000256|HAMAP-Rule:MF_01894};
GN OrderedLocusNames=Trebr_1569 {ECO:0000313|EMBL:AEE16992.1};
OS Treponema brennaborense (strain DSM 12168 / CIP 105900 / DD5/3).
OC Bacteria; Spirochaetota; Spirochaetia; Spirochaetales; Treponemataceae;
OC Treponema.
OX NCBI_TaxID=906968 {ECO:0000313|EMBL:AEE16992.1, ECO:0000313|Proteomes:UP000006546};
RN [1] {ECO:0000313|Proteomes:UP000006546}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 12168 / CIP 105900 / DD5/3
RC {ECO:0000313|Proteomes:UP000006546};
RA Lucas S., Han J., Lapidus A., Bruce D., Goodwin L., Pitluck S., Peters L.,
RA Kyrpides N., Mavromatis K., Ivanova N., Mikhailova N., Pagani I.,
RA Teshima H., Detter J.C., Tapia R., Han C., Land M., Hauser L.,
RA Markowitz V., Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Gronow S.,
RA Wellnitz S., Brambilla E., Klenk H.-P., Eisen J.A.;
RT "The complete genome of Treponema brennaborense DSM 12168.";
RL Submitted (APR-2011) 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. {ECO:0000256|HAMAP-
CC Rule:MF_01894}.
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DR EMBL; CP002696; AEE16992.1; -; Genomic_DNA.
DR RefSeq; WP_013758697.1; NC_015500.1.
DR AlphaFoldDB; F4LPD0; -.
DR STRING; 906968.Trebr_1569; -.
DR KEGG; tbe:Trebr_1569; -.
DR eggNOG; COG1196; Bacteria.
DR HOGENOM; CLU_001042_2_1_12; -.
DR OrthoDB; 9808768at2; -.
DR Proteomes; UP000006546; Chromosome.
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; 1.10.287.1490; -; 1.
DR Gene3D; 1.20.5.340; -; 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; IPR011890; SMC_prok.
DR PANTHER; PTHR42963; CHROMOSOME PARTITION PROTEIN MUKB; 1.
DR PANTHER; PTHR42963:SF1; CHROMOSOME PARTITION PROTEIN MUKB; 1.
DR Pfam; PF02463; SMC_N; 1.
DR PIRSF; PIRSF005719; SMC; 2.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|HAMAP-Rule:MF_01894};
KW Coiled coil {ECO:0000256|HAMAP-Rule:MF_01894};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_01894};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|HAMAP-
KW Rule:MF_01894}; Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01894};
KW Reference proteome {ECO:0000313|Proteomes:UP000006546}.
FT DOMAIN 2..917
FT /note="RecF/RecN/SMC N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02463"
FT REGION 950..977
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 167..201
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 269..338
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 381..408
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 522..777
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 977 AA; 110314 MW; 8FFD8A3D74C7BB34 CRC64;
MFLKSLEVFG FKSFADRTRI EFSDGITALL GPNGCGKSNV VDAVKWVLGE QGAKNMRAEK
MEDVIFNGTE TRKPLNVAEV TLTIANENGL LPLDVSEIMI KRRLYRSGES EYYINNAQVK
LKDVRELFWD TGVGKAAYSV MEQGKIDQIL SSKPEDRRYL FEEAAGITRF KVKRAEAERK
LERTEENMRQ VEGIMGEVKR SYDTLKVQAD KTISYRKFRD DIFNYELDIQ LLRLKNFTQD
RDRCAADAQK AANLRDGARA EIDAINASLS ENMEEVNAME GQLVSMQKEI YGLAVERNEK
DKQAKQLSER KAEAKAKVSQ LEGRFAALEE RIGSLREDID EQDAGLHAKR RRIDEITGNI
DSFQDNITLA GTQITENDRQ AAECEADIAA LDAERAELRK ELESITEDIV TELDSRLKDA
GYSSKVCTAA REKVDALLGK LAVLSSGRKN IFTDFASLAH PAEADVKRFA LNAVDAFTEA
ERLLAELGAA IGEYTASTPQ FIDEFLSPEG IITRKRSIDR KIQDSLDSVN RIRDRIAELK
SENAGLVGKI EEYRATLEQL RIQKAQMQTQ IEAAEDQIRI LRRELSLQEN SLRELENELF
TEKKRFDDIH EQLIEIEGEI ASIEYKGRSL TEKLEELERN ITSRNSDVSG KKEALSRKTA
DMAKFQSQLE KYTLDLATSE TEIRNIKDNF RETHSRDLME FEERMFTITV PAAELREKLA
ETRQQLKSLG SVNLMAPEEF AETKERHDFL AAQIADLQKA REDLQRITEE IRAESTELFL
ATYNKIKKNF HNMFRRLFGG GRAELRLVDP HNVLESGIDI FAQPPGKKLE NIALLSGGEK
TMTAVSLLFA TYMVRPSPFC LLDEIDAALD EQNVLRFVHT LRDFANVSQY IVITHNKKTV
SGAGTMLGVT MEESGVSKVI TIRLENEAGA GVGSLADPEP FIEEDVEPET DVYIPPHPPK
RIRPAAVSGE EGVHEET
//
