ID G7W112_PAETH Unreviewed; 1189 AA.
AC G7W112;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 27-MAR-2024, entry version 58.
DE RecName: Full=Chromosome partition protein Smc {ECO:0000256|HAMAP-Rule:MF_01894};
GN Name=smc {ECO:0000256|HAMAP-Rule:MF_01894};
GN OrderedLocusNames=HPL003_17975 {ECO:0000313|EMBL:AET60339.1};
OS Paenibacillus terrae (strain HPL-003).
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=985665 {ECO:0000313|EMBL:AET60339.1, ECO:0000313|Proteomes:UP000005876};
RN [1] {ECO:0000313|Proteomes:UP000005876}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HPL-003 {ECO:0000313|Proteomes:UP000005876};
RA Shin S.H., Kim S., Kim J.Y.;
RT "Complete sequence of Paenibacillus terrae HPL-003.";
RL Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=HPL-003;
RA Shin S.H., Kim S., Kim J.Y.;
RL Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:AET60339.1, ECO:0000313|Proteomes:UP000005876}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HPL-003 {ECO:0000313|EMBL:AET60339.1,
RC ECO:0000313|Proteomes:UP000005876};
RX PubMed=22328761; DOI=10.1128/JB.06668-11;
RA Shin S.H., Kim S., Kim J.Y., Song H.Y., Cho S.J., Kim D.R., Lee K.I.,
RA Lim H.K., Park N.J., Hwang I.T., Yang K.S.;
RT "Genome Sequence of Paenibacillus terrae HPL-003, a Xylanase-Producing
RT Bacterium Isolated from Soil Found in Forest Residue.";
RL J. Bacteriol. 194:1266-1266(2012).
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; CP003107; AET60339.1; -; Genomic_DNA.
DR RefSeq; WP_014281047.1; NC_016641.1.
DR AlphaFoldDB; G7W112; -.
DR STRING; 985665.HPL003_17975; -.
DR KEGG; pta:HPL003_17975; -.
DR eggNOG; COG1196; Bacteria.
DR HOGENOM; CLU_001042_2_2_9; -.
DR OrthoDB; 9808768at2; -.
DR Proteomes; UP000005876; 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; 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 COILED 167..201
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 262..296
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 339..483
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 682..828
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 878..940
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; 135030 MW; 9D077C49D811B7B4 CRC64;
MFLKRIELAG FKSFADKTEM EFVRGITAVV GPNGSGKSNI SDGIRWVLGE QSAKSLRGGK
MEDIIFAGSD ARKAVNYGEV SLTLDNEDQA LPLDFGEVTV TRRVHRSGDS EYFINRQSCR
LRDITELFMD TGIGKEAYSI IGQGRIEEIL STRSEDRRGI FEEASGIVKY KSRKKDAVRK
LDDTEQNLLR IHDLVSELED QIGPLKEQSE KAIHYKELRG ELKSKEISMY VHQIEQIHTS
WSDATSKLAL LQQEQLQLST VVSRHDAMLE SDRNELRQLE EQVERLQSDL LQYSEATEKS
EGYGELLKER TRNLEANREQ LILSLSTSES RHSERKSELD LLNEKLSALT VELDELRERL
SDEEAKLIGV TGGISQEQEE SLKGGLLELM NQMAQARNEI RYTDQQKEAL ERRVTRVSDE
SGKWEAQKAE LEQRKKGLET AVQKLGQEIS NLRSGYIQGS EKYQALQKML EESQGTVRKW
EQKREAQISR RDTMKEMQDD FEGFMLGVKE VLKAARKEAL HGVHGAVAEL IRVPEHLEQA
METALGASMQ HIVMENESVS RQAISFLKQR QLGRATFLPM DVIRPRQIGA GERQIVEGAE
GFVGIGADLV QYDERYAGIV GSLLGNVVIA RTLEDANRIA ARCQYRYRVV TLEGDVVNAG
GSMTGGSQFK KNANLLGRKR QLDQLDQDIM DTEQQIARLR QSAVDTKRQL EETQTRLDEL
RQGGDVKRGE EQQAAMELKQ LEHELRHVLE QVAASGQEKK GFDQEIKELE ASREEALLKL
AALEEEEKKT HQAIHAAEFA RKANESAKEQ LQGELTNLKV REGKLDQERF SLEEQLRRLR
GDYDTLGKDS RQNKTLLASI EADLLTNEQE SVKQIENLNQ YRLKKEEASQ QLEFKRAARS
SLSKKLEVAE NETKEQRIQL KSVEEQLRQT EIGVNRLDVE LENVLKKLSD DYELSYELAK
QRYPIPEDIE GTQAEVQRLK RGISALGEVN LGAIEEYQRV HERYTFLDEQ KSDLVEAKTT
LYQVIREMDD EMSKRFKTTF DAIRREFGTV FSKLFGGGRA DLVLIDPERM LETGIDIVAQ
PPGKKLQNLQ LLSGGERALT AMALLFAILH VKPVPFCVLD EVEAALDEAN VVRFAQYLRE
FSEQTQFIVV THRKGTMEEA DVLYGVTMEE GGVSKLVSVK LDNDEAEIA
//
