ID E1IEA5_9CHLR Unreviewed; 1192 AA.
AC E1IEA5;
DT 30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2010, sequence version 1.
DT 24-JAN-2024, entry version 57.
DE RecName: Full=Chromosome partition protein Smc {ECO:0000256|HAMAP-Rule:MF_01894};
GN Name=smc {ECO:0000256|HAMAP-Rule:MF_01894};
GN ORFNames=OSCT_1656 {ECO:0000313|EMBL:EFO80431.1};
OS Oscillochloris trichoides DG-6.
OC Bacteria; Chloroflexota; Chloroflexia; Chloroflexales; Chloroflexineae;
OC Oscillochloridaceae; Oscillochloris.
OX NCBI_TaxID=765420 {ECO:0000313|EMBL:EFO80431.1, ECO:0000313|Proteomes:UP000054010};
RN [1] {ECO:0000313|EMBL:EFO80431.1, ECO:0000313|Proteomes:UP000054010}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DG-6 {ECO:0000313|EMBL:EFO80431.1,
RC ECO:0000313|Proteomes:UP000054010};
RX PubMed=21037015; DOI=10.1128/JB.00931-10;
RA Kuznetsov B.B., Ivanovsky R.N., Keppen O.I., Sukhacheva M.V.,
RA Bumazhkin B.K., Patutina E.O., Beletsky A.V., Mardanov A.V., Baslerov R.V.,
RA Panteleeva A.N., Kolganova T.V., Ravin N.V., Skryabin K.G.;
RT "Draft genome sequence of the anoxygenic filamentous phototrophic bacterium
RT Oscillochloris trichoides subsp. DG-6.";
RL J. Bacteriol. 193:321-322(2011).
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:EFO80431.1}.
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DR EMBL; ADVR01000052; EFO80431.1; -; Genomic_DNA.
DR AlphaFoldDB; E1IEA5; -.
DR STRING; 765420.OSCT_1656; -.
DR eggNOG; COG1196; Bacteria.
DR HOGENOM; CLU_001042_2_2_0; -.
DR Proteomes; UP000054010; 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:UP000054010}.
FT DOMAIN 523..641
FT /note="SMC hinge"
FT /evidence="ECO:0000259|SMART:SM00968"
FT REGION 318..368
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 439..478
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 179..229
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 689..877
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 1005..1032
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COMPBIAS 318..342
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 352..368
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 446..478
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 36..43
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
SQ SEQUENCE 1192 AA; 131969 MW; 3D78EEC9313F6D68 CRC64;
MGPFMYLKRL DILGFKTFAT RTSVEFQPGI TAIVGPNGSG KSNIADAVRW VLGEQSLSTL
RCKRSEELIY SGGGRRAAAG LAEVSLTIDN SDRLLPLDFD EVTITRRATR AGENEYFINR
NRVRLRDLQA ATEPLGGSYT IINQGLVDAA LTLRPEERRR LFEDAAEIGG FDLRRAEALR
RLRETDANLQ RVADLLEELE PRLRVLKRQA GQARQYRELQ AELRTLLERH FASQWAQASA
ETARTRAEVE RMQHLLDHAR TAQLAASHEL RGLRESLRER REALGLLHQR SSDLHRRAET
LQRELAIDGE RLSALSRRGE DLERRQQELS TQHAEDEARR TQMLAEVQQS EAALEDQRHA
QRSAEAALAE SDRVRQMLGR ELRSTQEAAL KAAARVAEVA SRAEQVRTQT VRLEHDRSEL
AALATHTETQ VAQAQTHLAA TQTKLAEAED VRRSTAEQER SARSAREALR TERAQQEDQC
AAARRRVADL EARLESLTRL ARSYTGIFAG VRAAMQWAER SGRRGFALVQ TIIRTPAEIE
TAIEVALGSR LQHVVVEQWQ DAEEAINELK RTGAGRATFL PLDTIRGGGR SDLGGVKIDG
VAVLGVAADL VQYDQTYAPV VQQLLGRVLL VRDLATARAE LRRISGGWTI VTLHGEQVQS
GGAVTGGAQT KESGVLRRER ELRELPDQVA AARQHGAEAE ARRAEIEAQI QAQTQTLRSI
EVQLRESQRT LEVSRAAVDQ ATRRLAQAEQ ERGWAAQRQE RLAHDLRRLE DEAANLAEVH
TTATNAVTTA EAQLAEVRSR QETAAHADRQ AQEQLAELRA AVGAAEGQQR AQRTLLAAHE
RRLAETQHQL VAVRQSLAEL EQERAQIEQT HTRIKAEHHA LVEEIDQLRS AIDPAEQALA
ADETAQNELE QREQAATQTL LEQEAAYSRA AVEAQRASDR QDAIYERAAA EDIDVEALPI
PESAVPEANL PATIESLRSK IVRLGAVNQL ALEEYEEAAT RHRFLSEQVA DLRTAEASLQ
ELITELESAM NQRFTRTFHA VASEFEQSFV RLFGGGSAHL QLTGANSENG ADDSGSGHDQ
GVEIIVRPPG KKQQSIALLS GGERTLTAAA LLFAILKVNP SPFCILDETD AALDESNVGR
FREALAALVD QTQFILITHN RGTIEAADTL YGVTMGDDGA SKTFSLRVEV EI
//
