ID W4AUG1_9BACL Unreviewed; 1189 AA.
AC W4AUG1;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 24-JAN-2024, entry version 41.
DE RecName: Full=Chromosome partition protein Smc {ECO:0000256|HAMAP-Rule:MF_01894};
GN Name=smc {ECO:0000256|HAMAP-Rule:MF_01894};
GN ORFNames=C169_18974 {ECO:0000313|EMBL:ETT34471.1};
OS Paenibacillus sp. FSL R5-808.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=1227076 {ECO:0000313|EMBL:ETT34471.1, ECO:0000313|Proteomes:UP000019053};
RN [1] {ECO:0000313|EMBL:ETT34471.1, ECO:0000313|Proteomes:UP000019053}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FSL R5-808 {ECO:0000313|EMBL:ETT34471.1,
RC ECO:0000313|Proteomes:UP000019053};
RX PubMed=24422886; DOI=10.1186/1471-2164-15-26;
RA Moreno Switt A.I., Andrus A.D., Ranieri M.L., Orsi R.H., Ivy R.,
RA den Bakker H.C., Martin N.H., Wiedmann M., Boor K.J.;
RT "Genomic comparison of sporeforming bacilli isolated from milk.";
RL BMC Genomics 15:26-26(2014).
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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:ETT34471.1}.
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DR EMBL; ASPT01000032; ETT34471.1; -; Genomic_DNA.
DR RefSeq; WP_036642020.1; NZ_ASPT01000032.1.
DR AlphaFoldDB; W4AUG1; -.
DR PATRIC; fig|1227076.4.peg.3917; -.
DR Proteomes; UP000019053; 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: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; 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}.
FT DOMAIN 521..640
FT /note="SMC hinge"
FT /evidence="ECO:0000259|SMART:SM00968"
FT REGION 721..740
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 167..434
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 752..905
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; 135706 MW; 4EE2B9393F537F88 CRC64;
MFLKRIELAG FKSFADKTEM EFVRGITAVV GPNGSGKSNI SDGIRWVLGE QSAKSLRGGK
MEDIIFAGSD ARKAVNFGEV SLTLDNEDHV LPLDFNEVTV TRRVHRSGDS EYFINRQSCR
LKDITELFMD TGIGKEAYSI IGQGRIEEIL STRSEDRRGI FEEASGIVKY KSRKKESVRK
LDETEQNLLR IHDLVTELED QIGPLKEQSE KALRYKELRE ELKHKEISLY VYQIEQIHTS
WSEANAKLEQ LKEEQLALST VVSAHDAKLE SDRSALRRLE EEVEELQSQL LQFSELFEKS
EGYGEVLKER RRNLERTREQ LEESLHSGDH RLGERVGELA RMKNKLQELQ QELTHVRDQL
SAEEAKLVGV TGGISQQQEE SLKGNLLELM NQMAQARNEI RYADQQQEAL DRRMNRAQEE
SGKWEALKED LLKRKESIDR SIERFGKEIA DLRSGYISES ERYQSLQKLQ EETQGALRKW
EQKREAQISR RDTMKELQDD FDGFMLGVKE VLKASRKSVL QGVHGAVAEL IRVPEKLELA
METALGASVQ HIVMENESVS RQAIAFLKQR QLGRATFLPL DVIRPRNVSA SDRTLAEGEA
GFVGFGSELV QYDSRYSNIV GSLLGNVVIA ETLEQANKIA ARFSYRFRVV TLEGDVVNAG
GSMTGGSQHK KTNSLLGRKR QLEQLDQEIS ETEKQLEKLQ QGIESVRNQM VESQDKLDEL
RRAGDDKRVE EQQAAGDRKQ LDHELRHVLE QAELAGEEKS SHEKEAKEIQ ENRVRAQKLL
SELEDEEKST HLAIQAAEFA RKANESAKEE LQSQLTNLKV REGKLDQETF SLEEQLKRLQ
SDVDNHEKEQ KQNRTMLASV QADLNQNQSE SVKQIEDLNQ YKLKKEEATQ QLEFKRAARS
ALSRKLELEE SETKEQRTQL RAVDDQLRQT EIGVNRLDVE LENILKKLSE DYELSYELAK
QRYPIPEDIP AAQNEVRDLK RSITSLGDVN LGAIEEYQRV NERYLFLSEQ KADLVEAKTT
LYQVIKEMDD EMSKRFKLTF DAIRREFGTV FTKLFGGGRA DLVLIDPDRL LETGIDIVAQ
PPGKKLQNLQ LLSGGERALT AMALLFAILQ VKPVPFCVLD EVEAALDEAN VVRFAQYLRE
FSEQTQFIVV THRKGTMEEA DVLYGVTMEE GGVSKLVSVR LEDEEAEIA
//
