ID   SMC_AQUAE               Reviewed;        1156 AA.
AC   O66878;
DT   31-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 1.
DT   03-AUG-2022, entry version 127.
DE   RecName: Full=Chromosome partition protein Smc {ECO:0000255|HAMAP-Rule:MF_01894};
GN   Name=smc {ECO:0000255|HAMAP-Rule:MF_01894}; Synonyms=xcpC;
GN   OrderedLocusNames=aq_629;
OS   Aquifex aeolicus (strain VF5).
OC   Bacteria; Aquificae; Aquificales; Aquificaceae; Aquifex.
OX   NCBI_TaxID=224324;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VF5;
RX   PubMed=9537320; DOI=10.1038/32831;
RA   Deckert G., Warren P.V., Gaasterland T., Young W.G., Lenox A.L.,
RA   Graham D.E., Overbeek R., Snead M.A., Keller M., Aujay M., Huber R.,
RA   Feldman R.A., Short J.M., Olsen G.J., Swanson R.V.;
RT   "The complete genome of the hyperthermophilic bacterium Aquifex aeolicus.";
RL   Nature 392:353-358(1998).
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}.
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DR   EMBL; AE000657; AAC06839.1; -; Genomic_DNA.
DR   PIR; B70356; B70356.
DR   RefSeq; NP_213438.1; NC_000918.1.
DR   RefSeq; WP_010880376.1; NC_000918.1.
DR   AlphaFoldDB; O66878; -.
DR   SMR; O66878; -.
DR   STRING; 224324.aq_629; -.
DR   EnsemblBacteria; AAC06839; AAC06839; aq_629.
DR   KEGG; aae:aq_629; -.
DR   PATRIC; fig|224324.8.peg.512; -.
DR   eggNOG; COG1196; Bacteria.
DR   HOGENOM; CLU_001042_2_2_0; -.
DR   InParanoid; O66878; -.
DR   OMA; HNKIAME; -.
DR   OrthoDB; 1149850at2; -.
DR   Proteomes; UP000000798; 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; 2.
DR   PIRSF; PIRSF005719; SMC; 1.
DR   SMART; SM00968; SMC_hinge; 1.
DR   SUPFAM; SSF52540; SSF52540; 2.
DR   SUPFAM; SSF75553; SSF75553; 1.
DR   TIGRFAMs; TIGR02169; SMC_prok_A; 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..1156
FT                   /note="Chromosome partition protein Smc"
FT                   /id="PRO_0000409262"
FT   DOMAIN          509..624
FT                   /note="SMC hinge"
FT   COILED          167..499
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01894"
FT   COILED          654..1001
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01894"
FT   BINDING         37..44
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01894"
SQ   SEQUENCE   1156 AA;  135564 MW;  B12DB30F70C0CE49 CRC64;
     MEKRAYIEKI VVEGFKSYGT KRKEIPLGEG FIAVVGPNGA GKSNIGDAIS FALGLSSAKA
     LRAKNLSYLI FSKNGQKADH AYVEVHFKNL GAFPVEDEEV VISRKVSKDG RSIFKINGQV
     VRERDLKDFL AKAGIYETAY NVVYQGDIVK FLKMTPVERR KIIEEISGIG EYERKKEKAL
     EELAEVELKI KEIDLILEEI SNQLKRLKEE KEKLEKFKEL QRIKRETEAK ILLKEKEKLL
     KERERILNEL SSLRESLEDI TFQIQENEKE LNERERLLKE VNEKIMPFKE KVGKFTAEIE
     NAERSIKEKE RELKESENRV KNLEELINNL LSDKENLERE VGTLQLELEK LKEEYKSLKE
     VEREKLRELE EEEERLKITF DEVKKLEEEK EKLTEKLNSL NKEKQELEIQ RANLKNKIER
     IKEDINKLIS EREEKIKEIK EKEQEIKRLK AIKKKEEEEL RNLTQELNIY EKRLSEVRKK
     LEEVLKEKGA IEREVRSFSD VSDVFKDIKG VYGSVSELIR VKNPEHITAI EVAGGGRLKF
     IVVEDEEVAK ECIQLAKRMN LGRFSFIPLN RVRVEERPLR YPRTKGAVDF AVNLVEYDPK
     FEKVVKFVFG DTLIVENFES AKAIGIGNYR MVTLEGELFE KSGVITGGAV KPSGELNKRY
     YEEELQRLNA EEEKLKNEES IIQKKIREIR NLISEKTALL KVSERKIEEL SSEGLEQYEE
     KFKEKLENSK EYLKILEEKL LNVEDKLKEL AEEIEYYEEK LNNLKLKEGD IKRHYSREGV
     EEKRREYSKV RKQVSEIEKS LNEIERELNK KTYELEYLEK EIQEKERERE YLTERIKSLK
     KEIENLILFK EKTLQEVKEA EVKVYDYIKQ KEELEKEILN LKSKLGKLKI KEEELKEKIF
     EKEKNLKVLE EKIENLNEEL KEYEDLKLGA DEESIPKLKE KLKRVTEEIQ KLGSVNFRAE
     EDYAEELKRF NDYKEKQQKL KEESKAIKKL IEETENKKRK VFLEAFNQIN KSLKRIFSFL
     SPGGKAQMFL DNPEDPFSGG VQLTVKPRGK DVQYLEAMSG GEKTLAALSL IFALQEYKPS
     PFYYFDEVDA HLDEVNAKKV GELIREKSKE AQFIVVTLRE VVTSFADKIV GVSARGGISE
     VFFLKNEGLE EIIKEA