ID A0A0U3PNF9_9ACTN Unreviewed; 1195 AA.
AC A0A0U3PNF9;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE RecName: Full=Chromosome partition protein Smc {ECO:0000256|HAMAP-Rule:MF_01894};
GN Name=smc {ECO:0000256|HAMAP-Rule:MF_01894};
GN ORFNames=AS200_15455 {ECO:0000313|EMBL:ALV33269.1};
OS Streptomyces sp. CdTB01.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1725411 {ECO:0000313|EMBL:ALV33269.1, ECO:0000313|Proteomes:UP000068029};
RN [1] {ECO:0000313|EMBL:ALV33269.1, ECO:0000313|Proteomes:UP000068029}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CdTB01 {ECO:0000313|EMBL:ALV33269.1,
RC ECO:0000313|Proteomes:UP000068029};
RA Tian Y., Zhou G., Yang H., Lu X.;
RT "Complete genome sequence of the Streptomyces sp. strain CdTB01, a
RT bacterium tolerant to cadmium.";
RL Submitted (DEC-2015) 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; CP013743; ALV33269.1; -; Genomic_DNA.
DR RefSeq; WP_058922941.1; NZ_CP013743.1.
DR AlphaFoldDB; A0A0U3PNF9; -.
DR STRING; 1725411.AS200_15455; -.
DR KEGG; scx:AS200_15455; -.
DR OrthoDB; 9808768at2; -.
DR Proteomes; UP000068029; 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; 2.
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:SF2; STRUCTURAL MAINTENANCE OF CHROMOSOMES PROTEIN; 1.
DR PANTHER; PTHR43977; 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:UP000068029}.
FT DOMAIN 512..634
FT /note="SMC hinge"
FT /evidence="ECO:0000259|SMART:SM00968"
FT REGION 309..333
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 795..841
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 947..987
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 167..201
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 241..275
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 665..699
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 742..776
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COMPBIAS 315..333
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 804..841
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 965..987
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:0000256|HAMAP-Rule:MF_01894"
SQ SEQUENCE 1195 AA; 130080 MW; 13E31499B1E3FD92 CRC64;
MHLKALTLRG FKSFASATTL RFEPGITCVV GPNGSGKSNV VDALSWVMGE QGAKSLRGGK
MEDVIFAGTT GRPPLGRAEV SLTIDNSDGA LPIEYAEVTI TRIMFRNGGS EYQINGDTCR
LLDIQDLLSD SGIGREMHVI VGQGQLDSVL HADPMGRRAF IEEAAGVLKH RKRKEKALRK
LDAMQANLAR VQDLTDELRR QLKPLGRQAA VARRAAVIQA DLRDARLRLL ADDLVRLRQA
LQTEVADEAA LKERKEAAEQ ELRKALQREG LLEDEVRQLT PRLQRAQQTW YELSQLAERV
RGTISLADAR VKSATSAPPE ERRGRDPEDM EREAARIREQ EAELEAALEA AERALEDTVA
HRADLERELA QEERRLKDVA RAIADRREGL ARLGGQVNAA RSRAASAQAE IDRLAAARDE
AQERAVAAQE EYEALKAEVD ELDAGDTELA ERHEAAKAAL AEAEAQLSAA REAATAAERR
RAATQARHEA LAMGLRRKDG TGALLGAKDR LSGLLGPAAE LLTVTPGYEV ALAAAFGAAA
DALAVTSPAA AADAIRLLRK QDGGRAAFLL AGAGEDAPPR GAGNCAASHD GPEDATHTHA
ADLVRAPSDL LPAVRRILHG IVVVATLEDA QDLVYAHPHL TAVTAEGDLL GAHFAHGGSA
GAPSLLEVQA SVDEAAAELE ELAVRCEELT EAQHAAQERR GACTTLVEEL GERRRAADRE
KSAVAQQLGR LAGQARGAAG EAERSVAAAA RAQEALDKAL REVEELAERL AVAEEMPVEE
EPDTSVRDRL AADGANARQT EMEARLQVRT HEERVKGLAG RADSLDRAAR AERDARARAE
QRRARLRHEA AVAEAVASGT RQLLAHVEVS LRRAEEERAA AEAAKARRER ELAAARTAGR
DLKAELDKLT DSVHRGEVLG AEKRMRIEQL ETKALEELGV EPAGLVSEYG PHQLVPPSPP
AEGEELPEDP EHPRNRPKPF HRAEQERRLK AAERAYQQLG KVNPLALEEF AALEERHKFL
SEQLEDLKKT RADLLQVVKE VDERVEQVFT EAYRDTAREF EGVFSRLFPG GEGRLILTDP
DNMLTTGVDV EARPPGKKVK RLSLLSGGER SLTAVALLVS IFKARPSPFY VMDEVEAALD
DTNLQRLIRI MQELQEASQL IVITHQKRTM EVADALYGVS MQGDGVSKVI SQRLR
//
