ID A0A160FKX3_9BURK Unreviewed; 1172 AA.
AC A0A160FKX3;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 24-JAN-2024, entry version 29.
DE RecName: Full=Chromosome partition protein Smc {ECO:0000256|HAMAP-Rule:MF_01894};
GN Name=smc {ECO:0000256|HAMAP-Rule:MF_01894};
GN ORFNames=AYM40_12755 {ECO:0000313|EMBL:ANB73139.1};
OS Paraburkholderia phytofirmans OLGA172.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Paraburkholderia.
OX NCBI_TaxID=1417228 {ECO:0000313|EMBL:ANB73139.1, ECO:0000313|Proteomes:UP000076852};
RN [1] {ECO:0000313|EMBL:ANB73139.1, ECO:0000313|Proteomes:UP000076852}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OLGA172 {ECO:0000313|EMBL:ANB73139.1,
RC ECO:0000313|Proteomes:UP000076852};
RX PubMed=27063562; DOI=10.1016/j.gene.2016.04.018;
RA Ricker N., Shen S.Y., Goordial J., Jin S., Fulthorpe R.R.;
RT "PacBio SMRT assembly of a complex multi-replicon genome reveals
RT chlorocatechol degradative operon in a region of genome plasticity.";
RL Gene 586:239-247(2016).
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; CP014578; ANB73139.1; -; Genomic_DNA.
DR RefSeq; WP_063496540.1; NZ_CP014578.1.
DR AlphaFoldDB; A0A160FKX3; -.
DR STRING; 1804984.AYM40_12755; -.
DR KEGG; buz:AYM40_12755; -.
DR Proteomes; UP000076852; Chromosome 1.
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; 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; 2.
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};
KW Reference proteome {ECO:0000313|Proteomes:UP000076852}.
FT DOMAIN 518..625
FT /note="SMC hinge"
FT /evidence="ECO:0000259|SMART:SM00968"
FT REGION 403..429
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 170..211
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 244..362
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 729..901
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 988..1015
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT BINDING 32..39
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
SQ SEQUENCE 1172 AA; 129683 MW; 1AA002366C7E8FB8 CRC64;
MRLTSIKLAG FKSFVDPTHF QVPGQLVGVV GPNGCGKSNI IDAVRWVLGE SRASELRGES
MQDVIFNGST ARKPGSRASV ELVFDNADGR AAGQWGQYAE IAVKRVLTRD GTSSYYINNL
PARRRDIQDI FLGTGLGPRA YAIIGQGMIA RLIEAKPEEL RVFLEEAAGV SKYKERRRET
ENRLHDTREN LIRVEDIVRE LSANLEKLEA QAIVATRYKD LQADGEEKQR LLWLLRKNEA
GGEQERQQRA IEQAQIDLEA QTAKLREVEA QLETLRVAHY SASDAMQGAQ GALYEANAEV
SRLEAEIKFI VESRNRAQAQ IAALTAQREQ WQSQAQKAQD DLEDAEEQLA VAEEKAALAE
DEAAARHDAM PALEARWRDA QTELNAERGG IAQTEQALKL EAAHQRNADQ QLQQLQQRHE
RLKSEAGGLD APDEAQLEDM RAQLAEHEEI LHDAQARLAD AQETLPRLDG ERRAAQERVQ
SESAQIHQLD ARLAALKQLQ ENVQTEGKIQ PWLEKHELSG LPRLWKKLHV EAGWEAALEA
VLRERLAALE VSNLDWVKAF ATDAPPAKLA FYAPPAAGQP VTTPAGLRPL LSLVRIDDAG
IRAVLNDWLG LAFVADDLQQ ALAMRAQLPE GGSFVVKAGH VVTRVGVQLY AADSEQAGML
ARQQEIENLA RQVRAQALLA DEAKAAAIRA EAAHTQAAQA LTDVRQQSER ATQRVHALQM
DVLKLAQAHE RYTQRSTQIR EELEEITAQI DEQRALRGES EANFERHDAE LAELQARFED
HQLAFEALDE ALTAARAQSR DLDRAATDAR FAARNMANRI DELKRSIQVS HEQSERVAAS
LEDARAELET INEQTAHTGL QDALDIRAVK EEALHAARLE LEDLTAKLRA ADETRLTAER
ALQPLRDRIN ELQLKEQAAR LNGEQFIEQL AAAGVDEAEL QAKLTPDMKP SYLQGEVTRI
NNAITALGPV NMAALDELKA ATERKTFLDS QSADLNNAIE TLEDAIRKID GETRTLLQGT
FDEVNRHFGE LFPRLFGGGQ AKLIMTGDEI LDAGVQVMAQ PPGKKNSTIH LLSGGEKALT
ATALVFAMFQ LNPAPFCLLD EVDAPLDDAN TERFANLVRA MSDKTQFLFI SHNKIAMEMA
QQLIGVTMQE QGVSRIVAVD METAAGFAQN IV
//
