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Database: UniProt
Entry: E3EFZ4_PAEPS
LinkDB: E3EFZ4_PAEPS
Original site: E3EFZ4_PAEPS 
ID   E3EFZ4_PAEPS            Unreviewed;      1189 AA.
AC   E3EFZ4;
DT   11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT   11-JAN-2011, sequence version 1.
DT   27-MAR-2024, entry version 71.
DE   RecName: Full=Chromosome partition protein Smc {ECO:0000256|HAMAP-Rule:MF_01894};
GN   Name=smc {ECO:0000256|HAMAP-Rule:MF_01894,
GN   ECO:0000313|EMBL:ADO56027.1};
GN   ORFNames=PPSC2_09695 {ECO:0000313|EMBL:ADO56027.1};
OS   Paenibacillus polymyxa (strain SC2) (Bacillus polymyxa).
OC   Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX   NCBI_TaxID=886882 {ECO:0000313|EMBL:ADO56027.1, ECO:0000313|Proteomes:UP000006868};
RN   [1] {ECO:0000313|EMBL:ADO56027.1, ECO:0000313|Proteomes:UP000006868}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SC2 {ECO:0000313|EMBL:ADO56027.1,
RC   ECO:0000313|Proteomes:UP000006868};
RX   PubMed=21037012; DOI=10.1128/JB.01234-10;
RA   Ma M., Wang C., Ding Y., Li L., Shen D., Jiang X., Guan D., Cao F.,
RA   Chen H., Feng R., Wang X., Ge Y., Yao L., Bing X., Yang X., Li J., Du B.;
RT   "Complete genome sequence of Paenibacillus polymyxa SC2, a strain of plant
RT   growth-promoting Rhizobacterium with broad-spectrum antimicrobial
RT   activity.";
RL   J. Bacteriol. 193:311-312(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}.
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DR   EMBL; CP002213; ADO56027.1; -; Genomic_DNA.
DR   RefSeq; WP_013370642.1; NC_014622.2.
DR   AlphaFoldDB; E3EFZ4; -.
DR   STRING; 1406.LK13_22160; -.
DR   KEGG; ppm:PPSC2_09695; -.
DR   PATRIC; fig|886882.15.peg.2043; -.
DR   eggNOG; COG1196; Bacteria.
DR   HOGENOM; CLU_001042_2_2_9; -.
DR   OrthoDB; 9808768at2; -.
DR   Proteomes; UP000006868; 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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006868}.
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          332..483
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT   COILED          682..828
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT   COILED          878..926
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;  135090 MW;  E8103D313F81294C CRC64;
     MFLKRIELAG FKSFADKTEM EFVRGITAVV GPNGSGKSNI SDGIRWVLGE QSAKSLRGGK
     MEDIIFAGSD ARKAVNYGEV SLTLDNEDQA LPLDFGEVTV TRRVHRSGDS EYFINRQSCR
     LRDITELFMD TGIGKEAYSI IGQGRIEEIL STRSEDRRGI FEEASGIVKY KSRKKDAVRK
     LDETEQNLLR IHDLVSELED QIGPLKEQSE KAIHFKELRS ELKSKEISMY VHQIEQIHTS
     WSDATSKLAL LQQEQLQLST VVSRHDAMLE NDRNELRQLE EQVERLQKDL LQYSEATEKS
     EGYGELLKER TRNLEANREQ LILSLSTSES RHSERKSELD QLNEKLSALN VELDELRARL
     SDEEAKLIGV TGGISQEQEE SLKGGLLELM NQMAQARNEI RYTDQQKEAL ERRVNRVSDE
     SGKWEAQKVE LEQRKKGLEA TIQKLGQEIS SLRSGYIQGS EQYQALQKLL EENQGTVRKW
     EQKREAQISR RDTMKEMQDD FDGFMLGVKE VLKASRKGTL HGVHGAVAEL IRVPEHLEQA
     METALGASVQ HIVMENESVS RQAISFLKQR QLGRATFLPM DVIRPRQIGA GERQIVESAE
     GFVGIGADLV QYDDRYAGIV GSLLGNVVIA RTLEDANRIA ARCQYRYRVV TLEGDVVNAG
     GSMTGGSQFK KNANLLGRKR QLDQLDQDIL DTEQQIARLR QSAIDTKRQL EETQTRLDEL
     RQGGDVKRTE EQQMAMELKQ LEHELRHVLE QVAASGQEKK GFDQEIKELE ASRAEALVKL
     AALEEEEKKT HQAIHAAEFA RKANESAKEQ LQGELTNLKV REGKLDQERF SLEEQIRRLR
     GDYDTLGKDS RQNKTLLASI EADLLTNEQE TVKQIENLNQ YRLKKEEAAE QLEFKRAARS
     SLSKKLEVAE NDTKEQRIQL KSVEELLRQT EIGVNRLDVE LENVLKKLSD DYELSYELAK
     QRYPIPEDIE GTQSEVERLK RGISALGEVN LGAIEEYQRV HERYTFLDEQ KSDLVEAKTT
     LYQVIREMDD EMSKRFKTTF DAIRREFGTV FSKLFGGGRA DLVLLDPERL LETGIDIVAQ
     PPGKKLQNLQ LLSGGERALT AMALLFAILH VKPVPFCVLD EVEAALDEAN VVRFAQYLRE
     FSEQTQFIVV THRKGTMEES DVLYGVTMEE GGVSKLVSVK LDNDEAEIA
//
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