SMC_COXBU
ID SMC_COXBU Reviewed; 1169 AA.
AC Q81ZL2; Q7C3I8;
DT 31-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=Chromosome partition protein Smc {ECO:0000255|HAMAP-Rule:MF_01894};
GN Name=smc {ECO:0000255|HAMAP-Rule:MF_01894}; OrderedLocusNames=CBU_0540;
OS Coxiella burnetii (strain RSA 493 / Nine Mile phase I).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Legionellales; Coxiellaceae;
OC Coxiella.
OX NCBI_TaxID=227377;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=14660695; DOI=10.1093/molbev/msh023;
RA Cobbe N., Heck M.M.S.;
RT "The evolution of SMC proteins: phylogenetic analysis and structural
RT implications.";
RL Mol. Biol. Evol. 21:332-347(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RSA 493 / Nine Mile phase I;
RX PubMed=12704232; DOI=10.1073/pnas.0931379100;
RA Seshadri R., Paulsen I.T., Eisen J.A., Read T.D., Nelson K.E., Nelson W.C.,
RA Ward N.L., Tettelin H., Davidsen T.M., Beanan M.J., DeBoy R.T.,
RA Daugherty S.C., Brinkac L.M., Madupu R., Dodson R.J., Khouri H.M.,
RA Lee K.H., Carty H.A., Scanlan D., Heinzen R.A., Thompson H.A., Samuel J.E.,
RA Fraser C.M., Heidelberg J.F.;
RT "Complete genome sequence of the Q-fever pathogen, Coxiella burnetii.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:5455-5460(2003).
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 hinge near
CC the middle of the molecule. These domains are separated by coiled-coil
CC 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; AE016828; AAO90086.1; -; Genomic_DNA.
DR EMBL; AJ543641; CAD66594.1; -; Genomic_DNA.
DR RefSeq; NP_819572.1; NC_002971.3.
DR RefSeq; WP_010957646.1; NC_002971.4.
DR AlphaFoldDB; Q81ZL2; -.
DR SMR; Q81ZL2; -.
DR STRING; 227377.CBU_0540; -.
DR EnsemblBacteria; AAO90086; AAO90086; CBU_0540.
DR GeneID; 1208425; -.
DR KEGG; cbu:CBU_0540; -.
DR PATRIC; fig|227377.7.peg.533; -.
DR eggNOG; COG1196; Bacteria.
DR HOGENOM; CLU_001042_2_2_6; -.
DR OMA; HNKIAME; -.
DR Proteomes; UP000002671; 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; 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..1169
FT /note="Chromosome partition protein Smc"
FT /id="PRO_0000409269"
FT COILED 170..507
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01894"
FT COILED 659..1030
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 1169 AA; 133551 MW; A954FBE459169FFF CRC64;
MYLKTIKLAG FKSFVDPTLI PIRGSMNAIV GPNGCGKSNV VDAVRWVIGE TSAKQLRGQS
MSDVIFNGTT SRKPVGKASI ELHFDNSEGR IGGEYAKYGE IAIRREVERD GQSNYFINGA
HVRRRDVVDV FLGTGLGPRS YAIVEQGMIS NLIEAKPEEL RVYIEEAAGI SKYKERRRET
ESRMRHTQEN LDRVNDIAEE LAKQLRHLKR QANAAERYKA YKQEERALGA QFKVLQWKAL
DHKLSEHDQA INQKNTRREE KQSEQHRIET EIEKMREQLT DVNEKHNAVQ KRYYGLGADI
ARLEQRIKDT QEKIHQWQSE LEENENVWEE LQNNTAECEA QITELETELE HLKPRSSDIH
SAAAEASKEL AQAESNMARW QEAWEAFQAE TSQTMSQLEV MRTKREHCER QLTDLEKSKQ
QLQQNLKQLQ LDQLLNEIAP LSSQSELLNA ELSDSQSKLQ SLAETIASRR DANQTTREEL
QTQRRELQAL EARAASLEAL QKAALGESDG KISEWLSSQQ LKENPRLGQK LVVNPGWEIA
VETVLSGFFD AVCVDAALPF LTDLTTVSEG RVTLVEKKSV SASAFDKAPT LASQVKSEWP
FQQWLAGIYI ADTLDQAKQL QSSLQENESV ITKEGLWLGP HWARISKLQD APQSGFLLRE
QQLKQLKANI LGQQKKCDEQ EALLKSGEQQ LNQLETDRDT LLQTYQKLNA EATTVQSALS
TKQAQLDNAQ QQQTRLKIGL NECEQQIEQC QQQLTLIKNK ASSLDDSQGL LATRREEMIR
ERDHYRTQLI ELREKAHQKR KEADELEIRL ASNEDQLSLL RQTVARDQRQ LKQLTERREM
LSQYLSEGDK PLEELNEKLQ TQLEQRLILE TELREVEKEL EEANQLLRHL EEKRVSTQKA
LNEAQAQLEE LRMQRQTVSV RQTTIKEQLS ENDFDLEQVM AELPEEATIE SWQEKLDQLV
ERIQRMGPIN LAAIEEYESV NERKNYLDKQ HADLTEALEI LKNAIHKIDR ETRAKFQETY
DQVNQQFQSL FPRIFGGGRA TLEMTDTDLL TAGVIVRAQP PGKRNVTIHM LSGGEKALTA
VALVFSLFQL NPAPFCILDE VDAPLDDINV GRFCQLVKEM SKEVQFLVIS HNKVTIEMAD
YLMGVTMQEP GVSRIVSVNM QEAIGLVEA