ID C6E4M8_GEOSM Unreviewed; 1176 AA.
AC C6E4M8;
DT 01-SEP-2009, integrated into UniProtKB/TrEMBL.
DT 01-SEP-2009, sequence version 1.
DT 27-MAR-2024, entry version 73.
DE RecName: Full=Chromosome partition protein Smc {ECO:0000256|HAMAP-Rule:MF_01894};
GN Name=smc {ECO:0000256|HAMAP-Rule:MF_01894};
GN OrderedLocusNames=GM21_3299 {ECO:0000313|EMBL:ACT19324.1};
OS Geobacter sp. (strain M21).
OC Bacteria; Thermodesulfobacteriota; Desulfuromonadia; Geobacterales;
OC Geobacteraceae; Geobacter.
OX NCBI_TaxID=443144 {ECO:0000313|EMBL:ACT19324.1};
RN [1] {ECO:0000313|EMBL:ACT19324.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M21 {ECO:0000313|EMBL:ACT19324.1};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Saunders E., Brettin T., Detter J.C.,
RA Han C., Larimer F., Land M., Hauser L., Kyrpides N., Ovchinnikova G.,
RA Lovley D.;
RT "Complete sequence of Geobacter sp. M21.";
RL Submitted (JUL-2009) 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; CP001661; ACT19324.1; -; Genomic_DNA.
DR AlphaFoldDB; C6E4M8; -.
DR STRING; 443144.GM21_3299; -.
DR KEGG; gem:GM21_3299; -.
DR eggNOG; COG1196; Bacteria.
DR HOGENOM; CLU_001042_2_2_7; -.
DR OrthoDB; 9808768at2; -.
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; 1.10.287.1490; -; 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; PTHR42963; CHROMOSOME PARTITION PROTEIN MUKB; 1.
DR PANTHER; PTHR42963:SF1; CHROMOSOME PARTITION PROTEIN MUKB; 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|ARBA:ARBA00023125, ECO:0000256|HAMAP-
KW Rule:MF_01894}; Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01894}.
FT DOMAIN 524..633
FT /note="SMC hinge"
FT /evidence="ECO:0000259|SMART:SM00968"
FT COILED 198..271
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 300..348
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 433..502
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 674..820
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 990..1027
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 1176 AA; 132056 MW; 641FE677AEE75B6D CRC64;
MKIKRLEIHG FKSFQDKAVL DFNQPITGVV GPNGCGKSNV VDAIRWVMGE QSAKNLRGKS
MEDIIFGGTE FRKPLGMAEV SLFFSTEDGR VPAKYLNFSE IQVTRRLYRD GDSDYLLNKT
PCRLLDIAEL FMDTGIGAKA YSIIEQGKIG MILHAKPEER RFLIEEAAGV TKFKARKVVA
MKKMEATRQN LLRLGDIISE IKRQMNGLQR QAKKAERFRE IRLELKEIEL LFAAKGYGSV
QKERQGLERE IAELESKLVD VTARLNEAEL SIEGKRITLL ETERALTAAQ EEIFRWRSEL
QGGENKLEFQ RRELANQERH GARFEEELQG LRDQLAASER ELGSLEAQQT SFLEEHAREG
EALEHREALL EEMAASEAGV TRELDEARRA MFAALSEGAQ ANNQHAAAVK RLASIDERLQ
ASQRERVLLG ERLFESNGKV DALKAEREQL AREKELLDEE LTLAGSREAE LKQAQEAGEK
LLQQLRDQLS SASSRLKSLQ ELEAQFAGYG QGVKNLLLAD SFKGAPFTML ADAIEVEEEF
EVALESVLGE RLQYLLCGSP DLALDAVLHL KGNYGGRCSF ITAPPWHHPG DRPSGAAPLW
ERVTVPAQHA QLVEPLLSGA YLARDLAHAL ELAASFPHAT FVTVEGDLVH GGGILNGGSA
EPAQQGIIHK KREIKGLGAD VERLTGEVQQ LTEARETRRV EIAEAEAHRL ELRQSLHRLE
IRVLNAEKDL QSAQAECRRL EENAAVREME EEQFSEEKDL VAKEISQAEN RRGEAEERKL
ALEKNVEALQ GRLEGSRFEM EEAREMVTSL KVRVAALKEK GESTQRAYRR VEALCADLAS
RIASRGNELE GSGAERTRLI AAIAAGEEAL RDIVKQQLAS EQALLVVKER YETEAATVQE
EELRLKGTRS EASLLRDQLN AKSLRLTEVS MRLSHLEETL REKHRMEIAD ALLNYSKVEW
DEEERAARQA ELQKAINEMG EVNLMAIEEF KEMEERFSFL SSQKDDLEES MNALQKAIQR
INRTTRKRFL ETFQLVNEKF QTIFPRLFCG GHAELRLTDE EDLLNTGLDI VVQPPGKKLQ
NVSLLSGGEK ALTAVALIFS IFLIKPSPFC LLDEVDAPLD DANIGRFNDM VREMSANSQF
IIITHNRATM AVADTLYGVT MEEPGVSKLV SVRLNR
//
