SMC_CERS1
ID SMC_CERS1 Reviewed; 1151 AA.
AC A3PMS2;
DT 31-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT 31-MAY-2011, sequence version 2.
DT 03-AUG-2022, entry version 74.
DE RecName: Full=Chromosome partition protein Smc {ECO:0000255|HAMAP-Rule:MF_01894};
GN Name=smc {ECO:0000255|HAMAP-Rule:MF_01894};
GN OrderedLocusNames=Rsph17029_2536;
OS Cereibacter sphaeroides (strain ATCC 17029 / ATH 2.4.9) (Rhodobacter
OS sphaeroides).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC Rhodobacteraceae; Cereibacter.
OX NCBI_TaxID=349101;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 17029 / ATH 2.4.9;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Kiss H., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Richardson P.,
RA Mackenzie C., Choudhary M., Donohue T.J., Kaplan S.;
RT "Complete sequence of chromosome 1 of Rhodobacter sphaeroides ATCC 17029.";
RL Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Required for chromosome condensation and partitioning.
CC {ECO:0000255|HAMAP-Rule:MF_01894}.
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01894}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|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:0000255|HAMAP-Rule:MF_01894}.
CC -!- SIMILARITY: Belongs to the SMC family. {ECO:0000255|HAMAP-
CC Rule:MF_01894}.
CC -!- SEQUENCE CAUTION:
CC Sequence=ABN77638.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; CP000577; ABN77638.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_043828167.1; NC_009049.1.
DR AlphaFoldDB; A3PMS2; -.
DR SMR; A3PMS2; -.
DR EnsemblBacteria; ABN77638; ABN77638; Rsph17029_2536.
DR GeneID; 57471207; -.
DR KEGG; rsh:Rsph17029_2536; -.
DR HOGENOM; CLU_001042_2_2_5; -.
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:0006260; P:DNA replication; IEA:UniProtKB-UniRule.
DR GO; GO:0007062; P:sister chromatid cohesion; IEA:InterPro.
DR Gene3D; 3.40.50.300; -; 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 Pfam; PF02463; SMC_N; 1.
DR PIRSF; PIRSF005719; SMC; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR02168; SMC_prok_B; 1.
PE 3: Inferred from homology;
KW ATP-binding; Coiled coil; Cytoplasm; DNA-binding; Nucleotide-binding.
FT CHAIN 1..1151
FT /note="Chromosome partition protein Smc"
FT /id="PRO_0000409278"
FT REGION 421..483
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 806..826
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 862..889
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 170..218
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01894"
FT COILED 342..379
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01894"
FT COILED 407..508
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01894"
FT COILED 633..994
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01894"
FT COMPBIAS 421..482
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 864..889
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 32..39
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01894"
SQ SEQUENCE 1151 AA; 125439 MW; 42B4866EE05F9058 CRC64;
MRFTRLRLNG FKSFVDPTDL VIHEGLTGVV GPNGCGKSNL LEALRWVMGE NRPTAMRGAG
MEDVIFAGAA TRPARNFAEV ALVLDNADRL APAGFNDADT IEIVRRITRD AGSAYKANTK
DVRARDIQML FADASTGAHS PALVRQGQIS ELINAKPKAR RRILEEAAGI SGLYQRRHEA
ELRLAATEQN LARVEDVLDQ LAQQLSTLAR QAKQAARYRE IGEELRRAEG SLLYRRWREA
DLARTEALAI LRERMTAAGQ AEAAARKAAG ARAEAEATLP PKREEEAIAG AVLQRLTVER
DTLAAEEDRA RATIATLVSR VDQLGRDIER EAGLNRDAAE TIGRLEWERE ALETAHEGHE
ERLAEAAEAA REAGAALGER EEILSERTED AARLSARHQS AQRMLVDSRT TLARSEAEAA
RARETVEAAA EAQERAAETW EEAAAAQEEA QERAEAAEEA LVQADEARAE AQSREAEARA
QRSAAEGEAN ALRAEVAALA RLVDREAQAG SQLLDRIQVE PGFEAALGAA LSDDLRAPEV
AADAPSGWAA LPDYDETAPL PAGAEPLAPH VGVPEVLRRR IGQIGLVGRE AGAALQPLLQ
PGQRLVSIEG DLWRWDGFRA GAEDAPSAAA LRLKQLNRLV ALKRDLEEVA ARAEGARQAH
EALQARLAQL TRADQEAREA RRAADARVTE ASRAAARAEA DRSISGGKLE SARLAVKRYE
DEAMEARARL REAEGVASAL PDLEAARAGL EDLKMAVEAA RIAMMSRRSL HDELRREGEA
RVKRRQEVTK DLSGWKHRLE TAEKRSAELA ERKAETEEAL REAAEAPEEI AARREELAEA
IEAAEERRAR ASDALASAEA ALRAAQEAER EAERQAGESR EARARAEARA DAATEALQLA
AERIREETER TPQQLLEALA VDPERIPTVE ALETDVGRLK RQREALGAVN LRAEEDAQAV
QTEHDTLKAE KTDLEEAVKK LRAGIQGLNR EGRERLLTAF EQVNASFGTL FTHLFGGGEA
RLVMVESDDP LEAGLEIMCQ PPGKKLSTLS LLSGGEQTLT ALALIFAVFL ANPAPICVLD
EVDAPLDDAN VTRFCDLLDE MTRRTETRFL IITHHAVTMA RMDRLFGVTM AEQGVSQLVS
VDLKRAEALV A
