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Database: UniProt
Entry: K0K298_SACES
LinkDB: K0K298_SACES
Original site: K0K298_SACES 
ID   K0K298_SACES            Unreviewed;      1249 AA.
AC   K0K298;
DT   28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT   28-NOV-2012, sequence version 1.
DT   27-MAR-2024, entry version 56.
DE   RecName: Full=Chromosome partition protein Smc {ECO:0000256|HAMAP-Rule:MF_01894};
GN   Name=smc {ECO:0000256|HAMAP-Rule:MF_01894,
GN   ECO:0000313|EMBL:CCH34375.1};
GN   OrderedLocusNames=BN6_71400 {ECO:0000313|EMBL:CCH34375.1};
OS   Saccharothrix espanaensis (strain ATCC 51144 / DSM 44229 / JCM 9112 / NBRC
OS   15066 / NRRL 15764).
OC   Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC   Pseudonocardiaceae; Saccharothrix.
OX   NCBI_TaxID=1179773 {ECO:0000313|EMBL:CCH34375.1, ECO:0000313|Proteomes:UP000006281};
RN   [1] {ECO:0000313|EMBL:CCH34375.1, ECO:0000313|Proteomes:UP000006281}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51144 / DSM 44229 / JCM 9112 / NBRC 15066 / NRRL 15764
RC   {ECO:0000313|Proteomes:UP000006281};
RX   PubMed=22958348; DOI=10.1186/1471-2164-13-465;
RA   Strobel T., Al-Dilaimi A., Blom J., Gessner A., Kalinowski J.,
RA   Luzhetska M., Puhler A., Szczepanowski R., Bechthold A., Ruckert C.;
RT   "Complete genome sequence of Saccharothrix espanaensis DSM 44229T and
RT   comparison to the other completely sequenced Pseudonocardiaceae.";
RL   BMC Genomics 13:465-465(2012).
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}.
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DR   EMBL; HE804045; CCH34375.1; -; Genomic_DNA.
DR   AlphaFoldDB; K0K298; -.
DR   STRING; 1179773.BN6_71400; -.
DR   KEGG; sesp:BN6_71400; -.
DR   PATRIC; fig|1179773.3.peg.7214; -.
DR   eggNOG; COG1196; Bacteria.
DR   HOGENOM; CLU_001042_2_2_11; -.
DR   Proteomes; UP000006281; Chromosome.
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|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW   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|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_01894}; Reference proteome {ECO:0000313|Proteomes:UP000006281}.
FT   DOMAIN          518..631
FT                   /note="SMC hinge"
FT                   /evidence="ECO:0000259|SMART:SM00968"
FT   REGION          1193..1249
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          175..209
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT   COILED          247..283
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT   COILED          338..383
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT   COILED          426..495
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT   COILED          690..773
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT   COILED          805..839
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT   BINDING         40..47
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
SQ   SEQUENCE   1249 AA;  136348 MW;  3C4E2DB12459A55B CRC64;
     MVLGYAAPVH LKSLTLKGFK SFASATTLRF EPGITCVVGP NGSGKSNVLD ALRWVMGTQG
     AKDLRGGKME DVIFAGTSGR APLGRAEVTL TIDNSDGVLP IEYTEVSITR RMFREGATEY
     EINGSSCRLM DIQELLSDSG IGREMHVIVG QGQLAAILES KPEERRAFVE EAAGVLKHRK
     RKEKALRKLE AMQANLARLT DLTAELRRQL KPLGKQAEIA RRAQAVQSEL RDARMRLLAD
     DLVTRRAALA REEQDEATAR ARRTEVEQSL QQAQFQQNEL EDQVSADAPK LQQAQDTWYR
     LSALEERLRG TVRLAVERER HLSASVEAPR GGRDPDELDA EAEQTAELEQ ELQDAVTEAR
     IGLAEAVETR AELERVVQAA EKAHVAAVRA IADRREGLAR LSGQVEALRS KTSATAEEIE
     RMSVALAEAA ERAEVVAQEL AEAREVTGTE DEDDVGLDER HQRAVEANDA ARSRVEELVK
     AERTAERDIA SWQARVDALS LGLTRKDGAG ALLASRLPGL LGSVAALLTV EPGFEVALAA
     ALGPVADAVA VASGADALAA LELLKEQDAG RAGVLVGGSV PVDLPSWPVL PQGARWAVEL
     VRSPEALRPA LHRALDRLAV VDGLAGARDL VEAYPDVRAV TREGDVFGAD WAVGGSGRSQ
     SVIEVQAAVD EASEKLALTE RSLERSAAAL EGARAEQRAR RTEVDALKEQ LNEAKVRRAR
     SSERLNRLAA AVRSAQAEVE RVRVQREKVE AAREENLLKL GELEERLLVA EEQPLDDEPD
     TAQRDEAAAE LASARQGEVD ARLHLRTAEE RARAVQGRAE GLRRAARAER EARERAQRAH
     AARARGAVVA KAVVRGGEVA LARIGESLAR AARDRDVAQE RKAQRETFLT QVRSLVREMS
     VELEKLTDAV HRDEVLRAEQ RMRIEQLETK VAEDFGIGLD DLVAEYGPDV FIPPSQQEVA
     EYEAAKERGE AVTAPQPIPF DRDTQARRAK RAERDLSLLG KVNPLALEEF AALEERYKFL
     SNQLEDIKAT RRDLLTVVKE VDDKILEVFT SAYDDVAREF EVVFKVLFPG GEGRLVLTEP
     DDMLTTGIEL EARPPGKKVK RLSLLSGGEK SLAAVAMLVA IFRARPSPFY VMDEVEAALD
     DTNLHRLISL FEQLRERSQL LIITHQKPTM EIADALYGVS MRGDGISQVI SQRLRGRDDV
     RPAKSAPAAV PPPAEAPAVE TPVAAPAEVP AQEVPAEVVA EPAAGEPED
//
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