ID A0A0A1H412_9BURK Unreviewed; 1186 AA.
AC A0A0A1H412;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 24-JAN-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=E1O_08780 {ECO:0000313|EMBL:BAP88009.1};
OS Burkholderiales bacterium GJ-E10.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales.
OX NCBI_TaxID=1469502 {ECO:0000313|EMBL:BAP88009.1, ECO:0000313|Proteomes:UP000031649};
RN [1] {ECO:0000313|EMBL:BAP88009.1, ECO:0000313|Proteomes:UP000031649}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GJ-E10 {ECO:0000313|EMBL:BAP88009.1,
RC ECO:0000313|Proteomes:UP000031649};
RA Fukushima J., Tojo F., Asano R., Kobayashi Y., Shimura Y., Okano K.,
RA Miyata N.;
RT "Complete Genome Sequence of the Unclassified Iron-Oxidizing,
RT Chemolithoautotrophic Burkholderiales bacterium GJ-E10 Isolated from Acid
RT River.";
RL Submitted (NOV-2014) 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. SMC3 subfamily.
CC {ECO:0000256|ARBA:ARBA00005917}.
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DR EMBL; AP014683; BAP88009.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0A1H412; -.
DR STRING; 1469502.E1O_08780; -.
DR KEGG; bbag:E1O_08780; -.
DR HOGENOM; CLU_001042_2_2_4; -.
DR Proteomes; UP000031649; 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; 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; 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|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:UP000031649}.
FT DOMAIN 525..636
FT /note="SMC hinge"
FT /evidence="ECO:0000259|SMART:SM00968"
FT REGION 463..490
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 177..404
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 670..891
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 1007..1034
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COMPBIAS 475..490
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 39..46
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
SQ SEQUENCE 1186 AA; 132420 MW; F7B93B39871E9D51 CRC64;
MLFCERNVRL RQIKLAGFKS FVDPTQIDVP GQIVGVVGPN GCGKSNVIDA VRWVLGESKA
AELRGESMLD VIFNGSTERK PAGRASVELV FDNSEGRIGG EWSRFSELSV KRVLTRDNAS
AYLINQQQVR RRDVHDLFLG TGLGPRAYAI IGQGTISRIV EAKPEELRIF LEEAAGVSRY
KERRKETESR LADARDNLTR VEDVLRELDS QIERLHKQAE VAREYRTLTE RHRDAQSLLW
FTRREEGVAE QARRMREIEQ AETQLEAQMA DLRAVELRLV QERQAQDEAN AGAQAAQAEL
ARANEEVRKR DAQVRSTLES RAKLVAHGDA LAESRKRREA ELAQLVQRRA ELEREAGEAQ
ARLEAARAAC AEHEARVPEC EAAANAAREA VTAARAQAAS AQQAISGASA QMQGFDRQGN
ALAMRRERLS DEQSSLGAPD AARLDRLRAE IAALQADLDA AQAQGAQAEA QERELQGQRQ
TRTEERSKAS AELHRLDARL HAVRDTLAKM QADEKLDPWL RKQELQALPR LFARLEVDGG
WETAIEAVLR ERIEAIEVGR LEPMTAFGTM APPARVSFYA RAERELPPPA KAPWPRLAES
VRVRGGVESE GLRSVLEDWL AGVYVMPDLE QAMAARAELP AGAQFVVPGG HVVSRHGLRF
FAPEDRKAGL LAHRRDAENL ERQIKAQRLI DEQAAEALAR VEAQLRQAQE QARTARDRAA
QMRTRLHQLQ LESVRLAETI ERIRNRSGQI ESELEEIARE EAELNRHREE AETRFAQLDG
ELGRHQEAVE AARVQDEQAA ARLREARERL RQLESQRQRA EFDVTGLQDR RRDVDHGAGV
AAADIARLGE EIDRARLEAA KLDDSGVRGE LEEWLERQRQ AERAATDARS RFDEWMQRAR
ASDEQRQKIE RGLQPRRDRI TDLRLQEQAA RLAVEQFDRQ LAEVGVEGEP AREALHARLA
QAPAAAEQER EIARLAQAIS DLGAVNLAAL DELGAAQERQ GFLRTQSEDL RTAVETLEDA
IRKIDVESRA LLQETFDKVN GHFGEMFPRL FGGGQARLSM TGDEILDAGV QLTAQPPGKR
NSSIHLLSGG EKALTATALV FALFKLNPAP FCLLDEVDAP LDDANTERFC QLVRSMSDAT
QFLFISHNKI AMEMAQQLVG VTMQEQGVSR IVAVDLDSAV DMAESA
//
