ID   SMC_RHOPA               Reviewed;        1154 AA.
AC   Q6N1B7;
DT   31-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT   31-MAY-2011, sequence version 2.
DT   03-AUG-2022, entry version 105.
DE   RecName: Full=Chromosome partition protein Smc {ECO:0000255|HAMAP-Rule:MF_01894};
GN   Name=smc {ECO:0000255|HAMAP-Rule:MF_01894}; OrderedLocusNames=RPA4489;
OS   Rhodopseudomonas palustris (strain ATCC BAA-98 / CGA009).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Bradyrhizobiaceae; Rhodopseudomonas.
OX   NCBI_TaxID=258594;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-98 / CGA009;
RX   PubMed=14704707; DOI=10.1038/nbt923;
RA   Larimer F.W., Chain P., Hauser L., Lamerdin J.E., Malfatti S., Do L.,
RA   Land M.L., Pelletier D.A., Beatty J.T., Lang A.S., Tabita F.R.,
RA   Gibson J.L., Hanson T.E., Bobst C., Torres y Torres J.L., Peres C.,
RA   Harrison F.H., Gibson J., Harwood C.S.;
RT   "Complete genome sequence of the metabolically versatile photosynthetic
RT   bacterium Rhodopseudomonas palustris.";
RL   Nat. Biotechnol. 22:55-61(2004).
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAE29930.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; BX572607; CAE29930.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_042441319.1; NC_005296.1.
DR   AlphaFoldDB; Q6N1B7; -.
DR   SMR; Q6N1B7; -.
DR   STRING; 258594.RPA4489; -.
DR   PRIDE; Q6N1B7; -.
DR   EnsemblBacteria; CAE29930; CAE29930; RPA4489.
DR   GeneID; 66895634; -.
DR   KEGG; rpa:RPA4489; -.
DR   eggNOG; COG1196; Bacteria.
DR   HOGENOM; CLU_001042_2_2_5; -.
DR   BioCyc; RPAL258594:TX73_RS22940-MON; -.
DR   Proteomes; UP000001426; 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; IPR036277; SMC_hinge_sf.
DR   InterPro; IPR011890; SMC_prok.
DR   Pfam; PF02463; SMC_N; 1.
DR   PIRSF; PIRSF005719; SMC; 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..1154
FT                   /note="Chromosome partition protein Smc"
FT                   /id="PRO_0000409280"
FT   COILED          170..215
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01894"
FT   COILED          282..505
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01894"
FT   COILED          627..993
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   1154 AA;  126648 MW;  17038E235D3B5DEF CRC64;
     MKLTRLRLHG FKSFVEPTDF MIEPGLTGVV GPNGCGKSNL VEALRWAMGE TSHKSLRATD
     MDAVIFAGSG NRPARNHAEV VMSIDNSDRT APAALNDADT LDISRRIERE AGSVYRINGR
     EVRARDVQLL FADAATGARS PALVHQGKIG EIIQAKPEQR RRVLEDAAGV AGLHARRHEA
     ELRLKAAETN LTRVEDVIGQ LSTQVDGLKK QARQAIRFRE VAAKVRKTEA MLYHLRWRDA
     QAEVGAAAEV HDLGVRQLAE CTRVQAEASR IQADRASTLP SLREAEARAA AGLQRLINAR
     EQLDREEARA KERVVELERR LTQFSSDVAR EQQQAIDADA ALERLDTEDV ELREEILERV
     EKRSGVDERV AEADASLGEA EQLFAELTTQ LAELTARRNQ FEQSVRTHRD RLARLDTEIK
     NVESEIDRLS AETSGAGDLT ELAEAVEIAQ ELLAEQEGAV QEAEAAQIAA RQTLDGSRAP
     LVDAEKKVQR LETEAKTISK ILNGETKNLW PPIIDGITVA KGYEKAIGAV LGDDLDAPVD
     PSAPMRWTDV GVQPEDPALP EGVEALAQHV TAPPELARRL AQIGVVTKER GNELCEQLKT
     GQRLVSLDGD VWRWDGFVAS AHAPTGAARR LAERARLTDI ENELEQARIE ATAKRQALET
     AEADLKMAAA AETASRESLR GARREVDAAR ERFAAAEREV NRHAARKSAL AEAQSRLATD
     RAEAEAALEN AEAQIADLEP NTEAEARLAA VRGDIDGRRR IAAQIRAEAQ ALAREAELAD
     KRLQAIAAER MDWQKRKAGA ASQIATVEER VAELTAERAE LENAPEVFAE KRSAVITEIE
     FAEADRRAAA DALAAAEQAM SETDRLAKAS LEQLSSAREA CARAEERMEA ARRRLEDVER
     EIRDMLEVEP QAAAQLAEIV EGAELPPLAE IEESLDKLRR DRERLGAVNL RAEEELNEVE
     TQHGTLAAER DDLVEAIKKL RTGIQSLNKE ARERLLASFD VVNGHFKRLF TTLFGGGEAE
     LKLIESDDPL EAGLDIIAKP PGKKPQSLSL LSGGEQALTA MALIFAVFLT NPSPICVLDE
     VDAPLDDHNV ERFCDLLTDM AKTTETRFIT ITHNPITMAR MNRLFGVTMA ERGVSQLVSV
     DLQGAVDILD QNVA