ID H3SF22_9BACL Unreviewed; 1189 AA.
AC H3SF22;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 24-JAN-2024, entry version 46.
DE RecName: Full=Chromosome partition protein Smc {ECO:0000256|HAMAP-Rule:MF_01894};
GN Name=smc {ECO:0000256|HAMAP-Rule:MF_01894};
GN ORFNames=PDENDC454_10635 {ECO:0000313|EMBL:EHQ62341.1};
OS Paenibacillus dendritiformis C454.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=1131935 {ECO:0000313|EMBL:EHQ62341.1, ECO:0000313|Proteomes:UP000003900};
RN [1] {ECO:0000313|EMBL:EHQ62341.1, ECO:0000313|Proteomes:UP000003900}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C454 {ECO:0000313|EMBL:EHQ62341.1,
RC ECO:0000313|Proteomes:UP000003900};
RX PubMed=22461558; DOI=10.1128/JB.00158-12;
RA Sirota-Madi A., Olender T., Helman Y., Brainis I., Finkelshtein A.,
RA Roth D., Hagai E., Leshkowitz D., Brodsky L., Galatenko V., Nikolaev V.,
RA Gutnick D.L., Lancet D., Ben-Jacob E.;
RT "Genome Sequence of the Pattern-Forming Social Bacterium Paenibacillus
RT dendritiformis C454 Chiral Morphotype.";
RL J. Bacteriol. 194:2127-2128(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}.
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:EHQ62341.1}.
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DR EMBL; AHKH01000022; EHQ62341.1; -; Genomic_DNA.
DR RefSeq; WP_006676628.1; NZ_AHKH01000022.1.
DR AlphaFoldDB; H3SF22; -.
DR STRING; 1131935.PDENDC454_10635; -.
DR PATRIC; fig|1131935.3.peg.2180; -.
DR OrthoDB; 9808768at2; -.
DR Proteomes; UP000003900; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000003900}.
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..303
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 421..483
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 682..758
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 790..877
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 903..1031
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; 135387 MW; 388C5E2C78575F9F CRC64;
MFLKRLELAG FKSFADRTEL EFVQGITGVV GPNGSGKSNI SDAIRWVLGE QSAKSLRGGK
MEDIIFAGSD ARKAVNFGEV SLTLDNSDET LGLDFHEVTV TRRVHRSGDS EYFINKQPCR
LKDITELFMD TGIGKEAYSI IGQGRIEEIL STRSEDRRGI FEEASGIVKY KSRKRDAKKK
LDDTEQNLLR IHDLVVELED QIGPLKEQSE KARHFKQLKE MLKTKEIAVY VHQIEQLHTS
WQQANAKLSE LKERELALST VVSEHDSKLE VHRVELRKLE EELERLQATL LHYSEEYEKC
EGQGEVLRER KRNLVANEQQ MRASLATTSE RMRTKQLEVQ AVREKLLSLE SELVETKGLI
HAEEARLVGV TGGTSSDAEE SLKGELLDIM NQMAQQRNDI RYYDQQKEAL DKRLHKMKQG
RTKREQEQAD LRKRMEDAKR RMETMAEDLA YIRNRYLQES EQLKKDEALL GETEQAARKW
QQQADALVSR RDTMKELAND YDGFMLGVRE VLKAARRNSL QGVHGAVAEL IRVPEELETA
VETALGAALQ HIVMENEAVS RTAITFLKQR QLGRATFLPL DVIRSRTMNE SDRRAVEGAE
GYIGIAADLV RSDKAYANVV GSLLGNVVLA ETLEDANRIA ARLQYRYRIV TREGDVVNAG
GSMTGGSLNK KNANLLGRKR QLEQLDADIK ATDKQLTKLN ESVAELKKRT AAAVKRLDDL
REQGESKRIS EQQLASELTQ LEKEERQLAE LLEMEGQEFA HAAEEMTTLE SGRRTAELRL
SELKIEEDRL HVAIETAESA RKANESAKEE LQTQLTDMKV RQGKLEQETF SLQDRLKRVE
EEAHGYEQEY TQLTQSLIQV QIDLETAERE AMKQTEDLNH FGVKKQEAGK QIEFKRADRA
ASLERLEIAE SDTKEQRTEL KQVEEAMRQT EIQANRLDVE LDNLLRKLSD EYEISFELAK
HRYAMPDDIE AAQQEVRDLK RQISALGEVN LGAIEEYERI NERYQYLSEQ KDDLIEAKTA
LYQVIREMED EMSKRFKATF DEIRQRFVVV FAKLFGGGRA DLVLLEPDNI LETGIDIVAQ
PPGKKLQNLQ LLSGGERALT AMALLFAILH VKPVPFCVLD EVEAALDEAN VTRFAQYLRE
FAEVTQFIVV THRKGTMEEA DVLYGVTMEE GGVSKLVSVK LEDEEAIIA
//
