ID A0A1H7F2T0_9BACL Unreviewed; 1189 AA. AC A0A1H7F2T0; DT 22-NOV-2017, integrated into UniProtKB/TrEMBL. DT 22-NOV-2017, sequence version 1. DT 22-FEB-2023, entry version 13. DE RecName: Full=Chromosome partition protein Smc {ECO:0000256|HAMAP-Rule:MF_01894}; GN Name=smc {ECO:0000256|HAMAP-Rule:MF_01894}; GN ORFNames=SAMN05518856_10165 {ECO:0000313|EMBL:SEK20409.1}; OS Paenibacillus sp. OK003. OC Bacteria; Firmicutes; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus. OX NCBI_TaxID=1884380 {ECO:0000313|EMBL:SEK20409.1, ECO:0000313|Proteomes:UP000198837}; RN [1] {ECO:0000313|EMBL:SEK20409.1, ECO:0000313|Proteomes:UP000198837} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=OK003 {ECO:0000313|EMBL:SEK20409.1, RC ECO:0000313|Proteomes:UP000198837}; RA de Groot N.N.; RL Submitted (OCT-2016) 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. {ECO:0000256|HAMAP- CC Rule:MF_01894}. 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; FOBD01000001; SEK20409.1; -; Genomic_DNA. DR AlphaFoldDB; A0A1H7F2T0; -. DR EnsemblBacteria; SEK20409; SEK20409; SAMN05518856_10165. DR Proteomes; UP000198837; Unassembled WGS sequence. 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 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 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 TIGRFAMs; TIGR02168; SMC_prok_B; 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 521..640 FT /note="SMC hinge" FT /evidence="ECO:0000259|SMART:SM00968" FT COILED 167..201 FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894" FT COILED 234..299 FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894" FT COILED 325..483 FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894" FT COILED 682..947 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 1189 AA; 134956 MW; AB1EABCEC37D10C5 CRC64; MFLKRIELGG FKSFADKTEM EFVRGITAVV GPNGSGKSNI SDGIRWVLGE QSAKSLRGGK MEDIIFAGSD ARKAVNYGEV SLTLDNEDHA LALDFGEVTV TRRVHRSGDS EYFINKQSCR LKDITELFMD TGIGKEAYSI IGQGRIEEIL STRSEDRRGI FEEASGIVKY KSRKRDATRK LDETEQNLLR IHDLVTELED QIGPLKEQSE KAIHYKELRG QLKSQEISMY VYQIEQIHAS WSKANQRLES LKQEEVGLAA IVSTHDAKLE SDRNALRTLE TETEQLQSAL LQFSEATEKS EGLGELLKER SRHLQTNQEQ LKVTLAASEE RHREREAELL ALREKFTKLE LELSDVRNRL SEEEAKLIGV TGGISQQQEE SLKGNLLELM NQMAQTRNEI RYADQQKETL ERRMNRATEE SGKWEGQKET LEARKTEIEK KVVRLGKEIS DLRSGYITES ERLQSLQKLL EESRGTVRKW EQKREAQVSR RDTMKEMQDD FDGFMLGVKE VLKASRKGTL NGVHGAVAEL VKVPEKIELA VETAMGASLQ HVVMENESVS RQAIAFLKQR QLGRATFLPL DVIRARTIGA GERSMIEGMD GFVGIGADLV QYEERYAAII GSLLGNVIIA EKLEDANKIA ARCQYRFRVV TLEGDVVNAG GSMTGGSQHK KNGSLLSRKR QLDQLDQDIL DTENQIVKLH RSVDDVKTQL EQCQDKLDEL RQSGDDTRNA EQQASMEMKQ VEHELRHVLE QVAVAGQEKS GFTEEIKEMD TARDVAVKKL EQLEEEEKAT HRAIHAAEFA RKANESAKEE LQTQLTDLKV REGKLDQERF SNEEQLRRLE REVDSLVKDL RQNRTLLASM EADLKKTETE SVKQIEDLNQ YKLKKAESAQ ELDFKRAARS ELSKKLELAE SETKEQRTQL KAVEEQMRQT EISVNRLDVE LENILRKLMD EYELGYELAK ERYPVPEDVE STQAEVQKLK RSIAALGDVN LGAIEEFQRV NERYEFLSTQ KNDLVEAKTT LYQVIREMED EMAKRFKATF DAIRREFGAV FTKLFGGGRA DLVLMDPERL LDTGIDIVAQ PPGKKLQNLQ LLSGGERALT AMALLFAILH VKPVPFCVLD EVEAALDEAN VVRFAQYLRE FSEQTQFIVV THRKGTMEEA DVLYGVTMEE GGVSKLVSVK LEDEEAVIA //