SMC_RHOBA
ID SMC_RHOBA Reviewed; 1192 AA.
AC Q7UQV4;
DT 31-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT 31-MAY-2011, sequence version 2.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=Chromosome partition protein Smc {ECO:0000255|HAMAP-Rule:MF_01894};
GN Name=smc {ECO:0000255|HAMAP-Rule:MF_01894}; OrderedLocusNames=RB6065;
OS Rhodopirellula baltica (strain DSM 10527 / NCIMB 13988 / SH1).
OC Bacteria; Planctomycetes; Planctomycetia; Pirellulales; Pirellulaceae;
OC Rhodopirellula.
OX NCBI_TaxID=243090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 10527 / NCIMB 13988 / SH1;
RX PubMed=12835416; DOI=10.1073/pnas.1431443100;
RA Gloeckner F.O., Kube M., Bauer M., Teeling H., Lombardot T., Ludwig W.,
RA Gade D., Beck A., Borzym K., Heitmann K., Rabus R., Schlesner H., Amann R.,
RA Reinhardt R.;
RT "Complete genome sequence of the marine planctomycete Pirellula sp. strain
RT 1.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:8298-8303(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 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=CAD74592.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; BX294143; CAD74592.1; ALT_INIT; Genomic_DNA.
DR RefSeq; NP_867048.1; NC_005027.1.
DR AlphaFoldDB; Q7UQV4; -.
DR SMR; Q7UQV4; -.
DR STRING; 243090.RB6065; -.
DR EnsemblBacteria; CAD74592; CAD74592; RB6065.
DR KEGG; rba:RB6065; -.
DR PATRIC; fig|243090.15.peg.2925; -.
DR eggNOG; COG1196; Bacteria.
DR HOGENOM; CLU_001042_2_2_0; -.
DR InParanoid; Q7UQV4; -.
DR OrthoDB; 1149850at2; -.
DR Proteomes; UP000001025; Chromosome.
DR GO; GO:0005694; C:chromosome; IEA:InterPro.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IEA:InterPro.
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:0007165; P:signal transduction; IEA:InterPro.
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; IPR004089; MCPsignal_dom.
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..1192
FT /note="Chromosome partition protein Smc"
FT /id="PRO_0000409279"
FT DOMAIN 522..636
FT /note="SMC hinge"
FT COILED 164..197
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01894"
FT COILED 234..292
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01894"
FT COILED 333..369
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01894"
FT COILED 396..464
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01894"
FT COILED 676..736
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01894"
FT COILED 772..902
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01894"
FT COILED 986..1030
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01894"
FT BINDING 31..38
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01894"
SQ SEQUENCE 1192 AA; 131640 MW; 4E35C4EC20E8FE59 CRC64;
MLKALELAGF KSFADRTRFD FPDGITVVVG PNGSGKSNIV DAMKWVLGSQ SAKSLRGKDM
SDVIFKGSQT RGPAGAAEAT IIFDNTGGQM PVDAPEVHVT RRVYRSGEGE YLINQQAVRL
KDVKALIRGT GIGIDAYSLI EQGKVDRMLQ ANAKDRRAIF EEAAGISRFK AKKVEAERRL
ERVQTNLTRL GDIVDEVATR LKTLKSQAGK AERYRQASDR LKELRTVVAW NDWLTLSTEL
NEATTQLEAA QRQHRKADTL RESLEEQRQA AEMQLQTIAD AAREAEQSRS ELSGEIARIG
GRRESDQTTL VEQRRTLIGH YRRLRAMRTE AGSAIADLRK TIAALEVAEA ELADVQQKKE
SIAAKRDVEQ ATVHRIESAR DDLQRDHLAA VRRVAEHEAN RGRVAQQMRE AARALEEIAR
NSVTAEEGLK TALRDHDEVA RNVSELEKRI TDAQREVEIA DAKVCETRRV LERRREEIGS
LKIRLQGITE RARVLDELQQ KQEGVSGGVR EVLRMSNAEL KKDLVGIVAD CFSVDRQVAP
LIDAALGPRS QYVIVRGGSV SDAISRGDIK IGTRVGIIRL DELPNRRPGD KIRLDGLAGV
IGRADKMIDC EVELEPLVRH LLGNTWLVDT LATAIGLRKL SSAGLRFVTA SGDLLDNDGS
SVVGPPGGET GLVSRRSELA AAKSEMQHYS YQIAEAEKEV GRLTGVVDSE AAELGRHEQA
MRKWITEHAA AEAKLHHVTE RLSARQATVD ELKRSSASHT ELLATAKQQD GELAVSIQKG
KQEIETLEAQ RTEVDVQLTA ASEQLREVQS EAMSISVEAA RSEQRVESLT IAADVARRDQ
SQREAANQEV RDAMTRTRER ITEIETRILE ADNRLAELMI AMESADAKLQ VLAAEANQER
EATRRVQTES QAAIKAVAKA TEAVATISSA RDAAALKQST LADRIAEDYQ IDLRNDEPPE
ELAEIEDRSS VDEEISRLRG QVQNVGSVNM EALEELNELQ VRYDELHGQY QDLTAAKDSL
QRVIARINAD SRRLFLDTLE AIRINFQKLY RKSFGGGHAD LILEESDDPL EAGVEIVATP
PGKPSFSNSL LSGGEKALTA VALLMSIFQY RPSPFCVLDE VDAPFDEANI GRFVTVLTEF
LDQSKFIVVT HSKKTMTAAT TLYGVTMQES GVSKQVSIRF EDVSEDGQIN AA
