ID E3I0B2_RHOVT Unreviewed; 1152 AA.
AC E3I0B2;
DT 11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT 11-JAN-2011, sequence version 1.
DT 27-MAR-2024, entry version 63.
DE RecName: Full=Chromosome partition protein Smc {ECO:0000256|HAMAP-Rule:MF_01894};
GN Name=smc {ECO:0000256|HAMAP-Rule:MF_01894};
GN OrderedLocusNames=Rvan_3026 {ECO:0000313|EMBL:ADP72230.1};
OS Rhodomicrobium vannielii (strain ATCC 17100 / ATH 3.1.1 / DSM 162 / LMG
OS 4299).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Hyphomicrobiaceae; Rhodomicrobium.
OX NCBI_TaxID=648757 {ECO:0000313|EMBL:ADP72230.1, ECO:0000313|Proteomes:UP000001399};
RN [1] {ECO:0000313|Proteomes:UP000001399}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 17100 / ATH 3.1.1 / DSM 162 / LMG 4299
RC {ECO:0000313|Proteomes:UP000001399};
RX PubMed=21705585; DOI=10.1128/JB.05453-11;
RG US DOE Joint Genome Institute;
RA Brown P.J., Kysela D.T., Buechlein A., Hemmerich C., Brun Y.V.;
RT "Genome sequences of eight morphologically diverse alphaproteobacteria.";
RL J. Bacteriol. 193:4567-4568(2011).
CC -!- FUNCTION: Required for chromosome condensation and partitioning.
CC {ECO:0000256|HAMAP-Rule:MF_01894}.
CC -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_01894}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|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:0000256|HAMAP-Rule:MF_01894}.
CC -!- SIMILARITY: Belongs to the SMC family. {ECO:0000256|HAMAP-
CC Rule:MF_01894}.
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DR EMBL; CP002292; ADP72230.1; -; Genomic_DNA.
DR RefSeq; WP_013420599.1; NC_014664.1.
DR AlphaFoldDB; E3I0B2; -.
DR STRING; 648757.Rvan_3026; -.
DR KEGG; rva:Rvan_3026; -.
DR eggNOG; COG1196; Bacteria.
DR HOGENOM; CLU_001042_2_2_5; -.
DR OrthoDB; 9808768at2; -.
DR Proteomes; UP000001399; 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:0007059; P:chromosome segregation; IEA:UniProtKB-UniRule.
DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-UniRule.
DR GO; GO:0007062; P:sister chromatid cohesion; IEA:InterPro.
DR CDD; cd03278; ABC_SMC_barmotin; 1.
DR Gene3D; 1.20.5.170; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 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 PANTHER; PTHR43977; STRUCTURAL MAINTENANCE OF CHROMOSOMES PROTEIN 3; 1.
DR PANTHER; PTHR43977:SF1; STRUCTURAL MAINTENANCE OF CHROMOSOMES PROTEIN 3; 1.
DR Pfam; PF02463; SMC_N; 1.
DR PIRSF; PIRSF005719; SMC; 2.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF75553; Smc hinge domain; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|HAMAP-Rule:MF_01894};
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|HAMAP-
KW Rule:MF_01894};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_01894};
KW DNA-binding {ECO:0000256|HAMAP-Rule:MF_01894};
KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01894};
KW Reference proteome {ECO:0000313|Proteomes:UP000001399}.
FT DOMAIN 3..1135
FT /note="RecF/RecN/SMC N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02463"
FT COILED 170..231
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 293..410
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 438..465
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 630..768
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 797..824
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 874..901
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT BINDING 32..39
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
SQ SEQUENCE 1152 AA; 126726 MW; 51BA6CAAC7AEE539 CRC64;
MQITRLRLLG FKSFVEPTEL LIGPGLTGVV GPNGCGKSNL LEALRWVMGE TSYKTMRASA
MDDVIFAGTD KRPARNMAEV MVAVDNTKRT APAAFNDADV LEISRRIQRE AGSVYKVNGK
EVRAKDVQIL FADAATGARS QAMVQQGTIG QLINAKPQDR RRILEDAAGI AGLYTRRHEA
ELRLKAAEAN LERLKDVLGQ LGNQLSSLRR QARQAQKYRE LTTELRKLEA MQHHLHYSAA
NVAVQSEEAQ LLEALRAVGQ FTQAEAAALR LQAEAADALQ PLRDEEATRA AVLHRIEVER
NTLDREEARA KEREAELRAR LVQVQADAER EDAAIAEARE LLEKFDRDEE ALRALGDGSE
ARAETEARAE NAMEGLNEAE DALNVLTSKV AELRAERRQL EAQIAEHGGR AGRFAQQEAE
LSRQLADLRA RAEAASPVED LREDVAMLEA QIETIEGDII AAEEAVAAAR LREKDTRDAA
GAARLRAKSL ETEVATLIKL LKPSDAGRFK PIVDQISVSA GYEVALGAAL GDDLDVTADQ
TSPTRWTLVS DAGGDPALPY GAERLSNFVR GPLELSRRLA QIGVVASRDE GERLKASLAV
GQRLVTREGD LWRWDGFVSA ANAPSAAARR LAERNRLAGL EEQLDEVREA ADRAEAERLA
AQNAATEAQA SEKRLREAVR ASQAQLAQKR ATFSQAERAA MEEANKLRNI EEARERAAYA
REEAEAARED AQAALEEARP VDQAEAELAR LKERAAAARD VYTQAKAALD DIDRDIRARA
FRLKQIGEER LRWLQRTKSA NAQINSLAER LDGIRAELAE AEELPAKIAD RRNKILMEIG
QAETARKAAA DQLAAATNGL READRSLRDA QSGLSTARET RARIEARLEA ARERRAEYAN
AIRDTFECQP PEILSAVGLE DDATLPSPQE IEQQIVKLKA ERERLGGVNL RAEEEAAALG
GEFDGMEKER SDLQEAIGKL RTGIASLNKE GRKRLLEAFD TVQAHFVRLF QILFGGGEAE
LQLIESDDPL ESGLEIFCRP PGKKPQVLTL LSGGEKALTA LALIFAVFLT NPSPICVLDE
VDAPLDDANV DRFCTMMEEM ARSTETRFLV ITHHPMTMAR MNRLFGVTMQ EKGISQLVSV
DLQAAERFRE AS
//
