ID A0A0H3E0U6_BACA1 Unreviewed; 1186 AA.
AC A0A0H3E0U6;
DT 16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT 16-SEP-2015, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE RecName: Full=Chromosome partition protein Smc {ECO:0000256|HAMAP-Rule:MF_01894};
GN Name=smc {ECO:0000256|HAMAP-Rule:MF_01894};
GN OrderedLocusNames=BATR1942_05765 {ECO:0000313|EMBL:ADP32107.1};
OS Bacillus atrophaeus (strain 1942).
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=720555 {ECO:0000313|EMBL:ADP32107.1, ECO:0000313|Proteomes:UP000006867};
RN [1] {ECO:0000313|Proteomes:UP000006867}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1942 {ECO:0000313|Proteomes:UP000006867};
RA Gibbons H.S., Broomall S., McNew L.A., Daligault H., Chapman C., Bruce D.,
RA Karavis M., McGregor P., Hong C., Park K.H., Akmal A., Feldman A.,
RA Lin J.S., Chang W.E., Higgs B.W., Demirev P., Lindquist J., Liem A.,
RA Fochler E., Tapia R., Bishop-Lilly K., Detter C., Han C., Sozhamannan S.,
RA Rosenzweig C.N., Skowronski E.;
RT "Genomic signatures of strain selection and enhancement in Bacillus
RT atrophaeus subsp. Globigii, a historical biowarfare simulant.";
RL Submitted (SEP-2010) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ADP32107.1, ECO:0000313|Proteomes:UP000006867}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1942 {ECO:0000313|EMBL:ADP32107.1,
RC ECO:0000313|Proteomes:UP000006867};
RX PubMed=21464989; DOI=10.1371/journal.pone.0017836;
RA Gibbons H.S., Broomall S.M., McNew L.A., Daligault H., Chapman C.,
RA Bruce D., Karavis M., Krepps M., McGregor P.A., Hong C., Park K.H.,
RA Akmal A., Feldman A., Lin J.S., Chang W.E., Higgs B.W., Demirev P.,
RA Lindquist J., Liem A., Fochler E., Read T.D., Tapia R., Johnson S.,
RA Bishop-Lilly K.A., Detter C., Han C., Sozhamannan S., Rosenzweig C.N.,
RA Skowronski E.W.;
RT "Genomic signatures of strain selection and enhancement in Bacillus
RT atrophaeus var. globigii, a historical biowarfare simulant.";
RL PLoS ONE 6:E17836-E17836(2011).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP002207; ADP32107.1; -; Genomic_DNA.
DR RefSeq; WP_003328974.1; NC_014639.1.
DR AlphaFoldDB; A0A0H3E0U6; -.
DR GeneID; 23409676; -.
DR KEGG; bae:BATR1942_05765; -.
DR eggNOG; COG1196; Bacteria.
DR HOGENOM; CLU_001042_2_2_9; -.
DR OrthoDB; 9808768at2; -.
DR Proteomes; UP000006867; 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; 2.
DR Gene3D; 1.20.1060.20; -; 1.
DR Gene3D; 3.30.70.1620; -; 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; 2.
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}.
FT DOMAIN 518..637
FT /note="SMC hinge"
FT /evidence="ECO:0000259|SMART:SM00968"
FT COILED 167..201
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 262..475
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 679..727
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 756..860
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 896..923
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 994..1028
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 1186 AA; 135731 MW; 0AA466590BB98EB4 CRC64;
MFLKRLDVIG FKSFAERISV DFVKGVTAVV GPNGSGKSNI TDAIRWVLGE QSARSLRGGK
MEDIIFAGSD SRKRLNLAEV TLTLDNDDHF LPIDFHEVSV TRRVYRSGES EFLINNQPCR
LKDIIDLFMD SGLGKEAFSI ISQGKVEEIL SSKAEERRSI FEEAAGVLKY KTRKKKAENK
LFETQDNLNR VEDILHELEG QVEPLKIQAS IAKDYLDKKK ELEHVEIALT AYDIEELHGK
WTSLQKKVQI AKEEEVAESS AISAKEAKIE DTRDKIQALD ESVDELQQVL LVTSEELEKL
EGRKEVLKER KKNATQNREQ LEEAIILYQQ KETELKENIT KQTAVFEKLR AEVKQLQAQA
KEKQQALNLH SENVEEKIEQ LKSDYFELLN SQASFRNELQ LLDDQMSQSA VQQQRLTANN
EKYIQERKEI SEKKAACEAE FARIEHDMHR QVAQYREAQS KYEQKKRQYE KNESALYQAY
QFVQQAKSKK DMLETMQGDF SGFYQGVKEV LKAKNKLDGI HGAVLELITT EQTYETAIEI
ALGASAQHVI TENEQSARQA IQYLKQHSFG RATFLPLSVV KDRQLQSRDA ETAEKHPAFI
GVASDLVTFE PAYRRVIQNL LGTVLITEHL KGANELAKQL GHRYRIVTLE GDVVNPGGSM
TGGAVKKKNN SLLGRSRELE TITKRLVEME EKTALLESEV KSVKQSIQES ENKLAELREA
GENLRLKQQD IKGQLYELQI AEKNINTHLE LYDQEKSALL ENDQEKNARK RQLEKELAEV
SDQIKELEEE MERLTQQKQM QTSTKESLSN ELTEHKIAAA KKEQVCTNEE ENLNRLKKEL
EETQLALKET AEDLSFLTTE MSSSTSGEVK LEEAAKAKLN DKTRTAELIS VRRNQRMKLQ
QGLDTYELEL KEMKRLYKQK TTLLKDEEVK LGRMEVELDN LLQYLREEYS LSFEGAKEKY
QLETDPEEAR KRVKLIKLAI EELGTVNLGS IDEFERVNER YEFLSEQKND LTEAKNTLFQ
VIEEMDEEMT KRFNDTFVQI RSHFDHVFRS LFGGGRAELK LTDPNDLLHS GVDIIAQPPG
KKLQNLSLLS GGERALTAIA LLFSILKVRP VPFCVLDEVE AALDEANVFR FAQYLKKYSG
ETQFIVITHR KGTMEEADVL YGVTMQESGV SKLVSVKLEE TKELVQ
//
