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Database: UniProt
Entry: Q2SX06_BURTA
LinkDB: Q2SX06_BURTA
Original site: Q2SX06_BURTA 
ID   Q2SX06_BURTA            Unreviewed;      1170 AA.
AC   Q2SX06;
DT   24-JAN-2006, integrated into UniProtKB/TrEMBL.
DT   24-JAN-2006, sequence version 1.
DT   24-JAN-2024, entry version 114.
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:ABC36884.1};
GN   OrderedLocusNames=BTH_I2019 {ECO:0000313|EMBL:ABC36884.1};
OS   Burkholderia thailandensis (strain ATCC 700388 / DSM 13276 / CCUG 48851 /
OS   CIP 106301 / E264).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia; pseudomallei group.
OX   NCBI_TaxID=271848 {ECO:0000313|EMBL:ABC36884.1, ECO:0000313|Proteomes:UP000001930};
RN   [1] {ECO:0000313|EMBL:ABC36884.1, ECO:0000313|Proteomes:UP000001930}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700388 / DSM 13276 / CIP 106301 / E264
RC   {ECO:0000313|Proteomes:UP000001930};
RX   PubMed=16336651; DOI=10.1186/1471-2164-6-174;
RA   Kim H.S., Schell M.A., Yu Y., Ulrich R.L., Sarria S.H., Nierman W.C.,
RA   DeShazer D.;
RT   "Bacterial genome adaptation to niches: divergence of the potential
RT   virulence genes in three Burkholderia species of different survival
RT   strategies.";
RL   BMC Genomics 6:174-174(2005).
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; CP000086; ABC36884.1; -; Genomic_DNA.
DR   RefSeq; WP_009890424.1; NZ_CP008785.1.
DR   AlphaFoldDB; Q2SX06; -.
DR   KEGG; bte:BTH_I2019; -.
DR   HOGENOM; CLU_001042_2_2_4; -.
DR   OMA; HNKIAME; -.
DR   Proteomes; UP000001930; Chromosome I.
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; 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.
DR   SUPFAM; SSF57997; Tropomyosin; 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}.
FT   DOMAIN          518..625
FT                   /note="SMC hinge"
FT                   /evidence="ECO:0000259|SMART:SM00968"
FT   REGION          402..432
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          170..211
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT   COILED          251..278
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT   COILED          328..362
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT   COILED          694..901
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT   COILED          988..1019
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT   COMPBIAS        416..432
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   1170 AA;  129028 MW;  C60CDB2BEA2AC28D CRC64;
     MRLSSIKLAG FKSFVDPTHF QVPGQLVGVV GPNGCGKSNI IDAVRWVLGE SRASELRGES
     MQDVIFNGST ARKPGSRASV ELIFDNSDGR AAGQWGQYGE IAVKRVLTRD GTSSYYINNL
     PARRRDIQDI FLGTGLGPRA YAIIGQGMIA RIIEAKPEEL RVFLEEAAGV SKYKERRRET
     ENRLHDTREN LTRVEDIVRE LGANLEKLEA QAVVATKYKE LVADGEEKQR LLWLLRKNEA
     AAEQDKQRRA IGEAQIELDA QTAKLREVEA QLETLRVAHY SASDATQGAQ GALYEANAEV
     SRLEAEIKFI VESRNRVQSQ IAALVAQQEQ WRAQADKAQG DLEEAEEARA VADEKAAIAE
     DDAAAKHDAL PALEARWRDA QTGLNDERGR IAQTEQALKL EAAHQRNADQ QLQQLQQRHE
     RLKAEAGGLD APDEAQLEEL RMQLAEHEEI LGEAQARLAD AQETLPRLDA ERRAAHERVQ
     AESAQIHQLE ARLAALKQLQ ENVQTEGKIQ PWLDKHELGA LPRLWKKLHV EAGWETALEA
     VLRERLAALE VSNLDWVKAF ANDAPPAKLA FYAPPAAGEP LAAPGALRPL LPLVRIDDAG
     LRAVLNDWLG TVFVADDLAQ ALAARSQLPQ GGAFVVKAGH VVTRSGVQLY AADSEQAGML
     ARAQEIENLT RQVRAQALLS DEAKSAAIRA EAAHTQASQA LTEVRAQAER ATQRVHALQM
     DVLKLTQAHE RYTQRSTQIR EELEEIGAQI EEQRALRAES EANFERHDAE LAELQARFED
     NQLAFESLDE TLTNARQEAR ELERAATDAR FAARQSANRI DELKRSIQVA HEQAERVAAS
     LEDARAELET INEQTAHTGL QDALEVRAAK EQALGAARAE LDDLTAKLRA ADETRLAAER
     SLQPLRDRIT ELQLKEQAAR MTGEQFAEQL ATAEVDEAAL REKLTPDMKP SYLQGEVTRL
     NNAINALGPV NMAALEELAA ASERKVFLDA QSADLTNAIE TLEDAIRKID QETRALLQAT
     FDEVNRHFSD LFPRLFGGGQ AKLIMTGDEI LDAGVQVMAQ PPGKKNATIH LLSGGEKALT
     ATALVFAMFQ LNPAPFCLLD EVDAPLDDAN TERFANLVRA MSDKTQFLFI SHNKIAMEMA
     QQLIGVTMQE QGVSRIVAVD METAAGFAQN
//
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