SMC_BURP1
ID SMC_BURP1 Reviewed; 1170 AA.
AC Q3JR19;
DT 31-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT 31-MAY-2011, sequence version 2.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=Chromosome partition protein Smc {ECO:0000255|HAMAP-Rule:MF_01894};
GN Name=smc {ECO:0000255|HAMAP-Rule:MF_01894};
GN OrderedLocusNames=BURPS1710b_2592;
OS Burkholderia pseudomallei (strain 1710b).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia; pseudomallei group.
OX NCBI_TaxID=320372;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1710b;
RX PubMed=20333227; DOI=10.1093/gbe/evq003;
RA Losada L., Ronning C.M., DeShazer D., Woods D., Fedorova N., Kim H.S.,
RA Shabalina S.A., Pearson T.R., Brinkac L., Tan P., Nandi T., Crabtree J.,
RA Badger J., Beckstrom-Sternberg S., Saqib M., Schutzer S.E., Keim P.,
RA Nierman W.C.;
RT "Continuing evolution of Burkholderia mallei through genome reduction and
RT large-scale rearrangements.";
RL Genome Biol. Evol. 2:102-116(2010).
CC -!- FUNCTION: Required for chromosome condensation and partitioning.
CC {ECO:0000255|HAMAP-Rule:MF_01894}.
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01894}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|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 SMC hinge
CC near the middle of the molecule. These domains are separated by coiled-
CC coil structures. {ECO:0000255|HAMAP-Rule:MF_01894}.
CC -!- SIMILARITY: Belongs to the SMC family. {ECO:0000255|HAMAP-
CC Rule:MF_01894}.
CC -!- SEQUENCE CAUTION:
CC Sequence=ABA47647.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; CP000124; ABA47647.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_004527298.1; NC_007434.1.
DR AlphaFoldDB; Q3JR19; -.
DR SMR; Q3JR19; -.
DR PRIDE; Q3JR19; -.
DR EnsemblBacteria; ABA47647; ABA47647; BURPS1710b_2592.
DR KEGG; bpm:BURPS1710b_2592; -.
DR HOGENOM; CLU_001042_2_2_4; -.
DR OrthoDB; 1149850at2; -.
DR Proteomes; UP000002700; 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:0006260; P:DNA replication; IEA:UniProtKB-UniRule.
DR GO; GO:0007062; P:sister chromatid cohesion; IEA:InterPro.
DR Gene3D; 3.40.50.300; -; 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 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; SSF52540; 1.
DR SUPFAM; SSF75553; SSF75553; 1.
DR TIGRFAMs; TIGR02168; SMC_prok_B; 1.
PE 3: Inferred from homology;
KW ATP-binding; Coiled coil; Cytoplasm; DNA-binding; Nucleotide-binding.
FT CHAIN 1..1170
FT /note="Chromosome partition protein Smc"
FT /id="PRO_0000409265"
FT DOMAIN 520..623
FT /note="SMC hinge"
FT COILED 169..215
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01894"
FT COILED 245..365
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01894"
FT COILED 401..508
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01894"
FT COILED 664..944
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01894"
FT COILED 983..1020
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01894"
FT BINDING 32..39
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01894"
SQ SEQUENCE 1170 AA; 129041 MW; D2A219E3AEF0B32A CRC64;
MRLSSIKLAG FKSFVDPTHF QVPGQLVGVV GPNGCGKSNI IDAVRWVLGE SRASELRGES
MQDVIFNGST TRKPGSRASV ELIFDNSDGR AAGQWGQYGE IAVKRVLTRD GTSSYYINNL
PARRRDIQDI FLGTGLGPRA YAIIGQGMIA RIIEAKPEEL RVFLEEAAGV SKYKERRRET
ENRLHDTREN LTRVEDIVRE LGANLEKLEA QAVVATKYKE LVADGEEKQR LLWLLRKNEA
AAEQDRQRRA IGDAQIELDA QTAKLREVEA QLETLRVAHY SASDAMQGAQ GALYEANAEV
SRLEAQIKFI VESRNRVQAQ IAALVAQQEQ WRAQADKAQG DLEVAEEARA VADEKAAIAE
DDAAAKHDAL PALEARWRDA QTGLNDERGR IAQTEQALKL EAAHQRNADQ QLQQLQQRHE
RLKVEAGGLD APDEAQLEEL RMQLAEHEAM LAEAQARLAD AQEALPRLDA QRRAAHERVQ
AESAQIHQLE ARLAALKQLQ ENVQTQGKIQ PWLDKHELGA LPRLWKKLHV EAGWETALEA
VLRERLAALE VSNLDWVKAF ATDAPPAKLA FYAPPAAGEP LAAPGALRPL LPLVRIDDAG
LRAVLNDWLG TVFVADDLAQ ALAARMQLPQ GGAFVVKAGH VVTRSGVQLY AADSEQAGML
ARAQEIENLT RQVRAQALLS DEAKAAAIRA EAAHTQASQA LTEVRAQAER ATQRVHALQM
DVLKLTQAHE RYTQRSTQIR EELEEIGAQI EEQRALRAES EANFERHDAE LAELQARFED
NQLAFESLDE TLTNARQEAR ERERAATDAR FAARQSANRI DELKRSIQVA HEQAERVAAS
LEDARAELET INEQTAHTGL QDALEVRAAK EQALGAARAE LDDLTAKLRA ADEARLAAER
SLQPLRDRIT ELQLKEQAAR MTGEQFAEQL ATAEVDEAAL KEKLMPDMKP SYLQGEVTRI
NNAINALGPV NMAALDELAA ASERKVFLDA QSADLTNAIE TLEDAIRKID QETRALLQAT
FDEVNRHFSD LFPRLFGGGQ AKLIMTGDEI LDAGVQVMAQ PPGKKNATIH LLSGGEKALT
ATALVFAMFQ LNPAPFCLLD EVDAPLDDAN TERFANLVRA MSDKTQFLFI SHNKIAMEMA
QQLIGVTMQE QGVSRIVAVD METAAGFAQN