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
//