SMC_FUSNN
ID SMC_FUSNN Reviewed; 1183 AA.
AC Q8REH4;
DT 31-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT 31-MAY-2011, sequence version 2.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=Chromosome partition protein Smc {ECO:0000255|HAMAP-Rule:MF_01894};
GN Name=smc {ECO:0000255|HAMAP-Rule:MF_01894}; OrderedLocusNames=FN1129;
OS Fusobacterium nucleatum subsp. nucleatum (strain ATCC 25586 / DSM 15643 /
OS BCRC 10681 / CIP 101130 / JCM 8532 / KCTC 2640 / LMG 13131 / VPI 4355).
OC Bacteria; Fusobacteria; Fusobacteriales; Fusobacteriaceae; Fusobacterium.
OX NCBI_TaxID=190304;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25586 / DSM 15643 / BCRC 10681 / CIP 101130 / JCM 8532 / KCTC
RC 2640 / LMG 13131 / VPI 4355;
RX PubMed=11889109; DOI=10.1128/jb.184.7.2005-2018.2002;
RA Kapatral V., Anderson I., Ivanova N., Reznik G., Los T., Lykidis A.,
RA Bhattacharyya A., Bartman A., Gardner W., Grechkin G., Zhu L., Vasieva O.,
RA Chu L., Kogan Y., Chaga O., Goltsman E., Bernal A., Larsen N., D'Souza M.,
RA Walunas T., Pusch G., Haselkorn R., Fonstein M., Kyrpides N.C.,
RA Overbeek R.;
RT "Genome sequence and analysis of the oral bacterium Fusobacterium nucleatum
RT strain ATCC 25586.";
RL J. Bacteriol. 184:2005-2018(2002).
CC -!- FUNCTION: Required for chromosome condensation and partitioning.
CC {ECO:0000255|HAMAP-Rule:MF_01894}.
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01894}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|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 SMC hinge
CC near the middle of the molecule. These domains are separated by coiled-
CC coil structures. {ECO:0000255|HAMAP-Rule:MF_01894}.
CC -!- SIMILARITY: Belongs to the SMC family. {ECO:0000255|HAMAP-
CC Rule:MF_01894}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAL95325.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AE009951; AAL95325.1; ALT_INIT; Genomic_DNA.
DR RefSeq; NP_604026.1; NC_003454.1.
DR AlphaFoldDB; Q8REH4; -.
DR SMR; Q8REH4; -.
DR STRING; 190304.FN1129; -.
DR PRIDE; Q8REH4; -.
DR EnsemblBacteria; AAL95325; AAL95325; FN1129.
DR KEGG; fnu:FN1129; -.
DR PATRIC; fig|190304.8.peg.1694; -.
DR eggNOG; COG1196; Bacteria.
DR HOGENOM; CLU_001042_2_2_0; -.
DR InParanoid; Q8REH4; -.
DR Proteomes; UP000002521; 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:0006260; P:DNA replication; IEA:UniProtKB-UniRule.
DR GO; GO:0007062; P:sister chromatid cohesion; IEA:InterPro.
DR Gene3D; 3.40.50.300; -; 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 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; SSF52540; 1.
DR SUPFAM; SSF75553; SSF75553; 1.
DR TIGRFAMs; TIGR02168; SMC_prok_B; 1.
PE 3: Inferred from homology;
KW ATP-binding; Coiled coil; Cytoplasm; DNA-binding; Nucleotide-binding;
KW Reference proteome.
FT CHAIN 1..1183
FT /note="Chromosome partition protein Smc"
FT /id="PRO_0000409272"
FT DOMAIN 519..632
FT /note="SMC hinge"
FT COILED 162..483
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01894"
FT COILED 666..1019
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01894"
FT BINDING 32..39
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01894"
SQ SEQUENCE 1183 AA; 136414 MW; 1302E0439A333D2D CRC64;
MYLKAVEING FKSFGDKVYI DFNRGITSIV GPNGSGKSNI LDAVLWVLGE QSYKNIRAKE
SQDVIFSGGK EKKPATKAEV SLIIDNADRY LDLDNDTVKI TRRIHISGEN EYLINDTKSR
LKEIGTLFLD TGIGKTAYSV IGQGKVERII NSSPKEIKSI IEEAAGIKKL QANRIEAQKN
LANIEINLDK VEFILNETRE NKNKIEKQAE LAQKYIDLRD EKSSLAKGIY ITELEQKEKN
LSENENIKEK YQTECFELQE KLNKTLERLN TIDLEKEEVK KEKLLIDSRN KELRNIISEK
EKEKAVTSER LDNVKKEKLV KEEYILHLDN KIEKKLEEVT ESKNKKDEIS KNIVEMAAAN
KEFENKIFNL ENIKVEKFDL IENRAKKVRD LELEKQLASN EIENNEKKLK SSQDEVENFK
QELEEANKKL LANNKEKDLV HSQLEARKEE LTKTEERNEF LVNQLSEISK SINKLSQDIR
EFEYQEKTSS GKLEALVRMD ENNEGFFKGV KEVLNSGISG IDGVLISLIN FDEKYEKAVE
AAIPGNLQDI IVEDKEVAKK CIAFLTEKKL GRTSFLALDT IKPNRREFKA NINGVLGLTA
DLITADKKYQ KVIDFIFGGL LIVENIDIAT DILNKNLFSG NIVTLTGELV SSRGRITGGE
NQKSTINQIF ERKKEIKTLE EKVTDLKSKI TEGSKKREDL SIKLENYENE VDKIDSLEDS
IRKDIDLLKK DFESLSEKSE KLSKDIRSIS FNIEDAEKYK TSYQDRINSS FSTIEETEKH
IASLKKDIEA DENLLKQTIS EIDSLNKQFS DTRILFLNNQ STIEQLEKDI HSKEIENVEL
QEEKEKNSKI VIELSHNIEE LETLEEELQS QIEEHTKIYN SENRDIETLN EREQNLSNEE
RELSKDKSKL ETDSLHANDR FEKIVEVIEK IKVDILNINE KLNELVEITA QVIEVEKLKS
SKDRLRSLEN KINNFGDVNL LAINEFKELK ERYDYLARER DDVVKSRKQV MDLIQEIDER
IHEDFHTTYQ NINENFNKMC DETIRNTEGR LNIINPEDFE NCGIEIFVKF KNKKKQPLSL
LSGGEKSMVA IAFIMAIFMY KPSPFTFLDE IEAALDEKNT KNLLGKLRDF TDKSQFILIT
HNKETMKESD SIFGVTMNKE IGISKIVSPD KITKILSENK ENN
