ID Q12AD2_POLSJ Unreviewed; 1182 AA.
AC Q12AD2;
DT 22-AUG-2006, integrated into UniProtKB/TrEMBL.
DT 22-AUG-2006, sequence version 1.
DT 27-MAR-2024, entry version 105.
DE RecName: Full=Chromosome partition protein Smc {ECO:0000256|HAMAP-Rule:MF_01894};
GN Name=smc {ECO:0000256|HAMAP-Rule:MF_01894};
GN OrderedLocusNames=Bpro_2594 {ECO:0000313|EMBL:ABE44510.1};
OS Polaromonas sp. (strain JS666 / ATCC BAA-500).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Polaromonas.
OX NCBI_TaxID=296591 {ECO:0000313|EMBL:ABE44510.1, ECO:0000313|Proteomes:UP000001983};
RN [1] {ECO:0000313|Proteomes:UP000001983}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JS666 / ATCC BAA-500 {ECO:0000313|Proteomes:UP000001983};
RX PubMed=18723656; DOI=10.1128/AEM.00197-08;
RA Mattes T.E., Alexander A.K., Richardson P.M., Munk A.C., Han C.S.,
RA Stothard P., Coleman N.V.;
RT "The genome of Polaromonas sp. strain JS666: insights into the evolution of
RT a hydrocarbon- and xenobiotic-degrading bacterium, and features of
RT relevance to biotechnology.";
RL Appl. Environ. Microbiol. 74:6405-6416(2008).
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. SMC3 subfamily.
CC {ECO:0000256|ARBA:ARBA00005917}.
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DR EMBL; CP000316; ABE44510.1; -; Genomic_DNA.
DR RefSeq; WP_011483508.1; NC_007948.1.
DR AlphaFoldDB; Q12AD2; -.
DR STRING; 296591.Bpro_2594; -.
DR KEGG; pol:Bpro_2594; -.
DR eggNOG; COG1196; Bacteria.
DR HOGENOM; CLU_001042_2_2_4; -.
DR OrthoDB; 9808768at2; -.
DR Proteomes; UP000001983; 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; 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; IPR010935; SMC_hinge.
DR InterPro; IPR011890; SMC_prok.
DR NCBIfam; TIGR02168; SMC_prok_B; 1.
DR PANTHER; PTHR43977; STRUCTURAL MAINTENANCE OF CHROMOSOMES PROTEIN 3; 1.
DR PANTHER; PTHR43977:SF1; STRUCTURAL MAINTENANCE OF CHROMOSOMES PROTEIN 3; 1.
DR Pfam; PF06470; SMC_hinge; 1.
DR Pfam; PF02463; SMC_N; 1.
DR PIRSF; PIRSF005719; SMC; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|HAMAP-Rule:MF_01894};
KW Coiled coil {ECO:0000256|HAMAP-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:UP000001983}.
FT DOMAIN 3..1164
FT /note="RecF/RecN/SMC N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02463"
FT DOMAIN 523..632
FT /note="SMC hinge"
FT /evidence="ECO:0000259|Pfam:PF06470"
FT COILED 170..255
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 363..411
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 451..478
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 696..786
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 822..952
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 1182 AA; 131183 MW; D6D8B8242B33251D CRC64;
MRLNSIKLSG FKSFAEPTNF VLPGQLVGVV GPNGCGKSNI MDAVRWVLGE SKASELRGES
MQDVIFNGTN TRKPASRSSV ELVFDNADHR AGGQWGQFAE IAVKRVLTRD GTSSYYINNQ
PVRRRDVQDV FLGTGLGPRA YAIIGQGTIS RIIESKPEEL RLFLEEAAGV SKYKERRRET
ANRLSDTREN LTRVEDILRE LNANLDRLEK QAEVAMRYNT LQADSTLKQH QLWFLKRAES
QADQARVKVD SEKAVNDLES RVADLRHIEA DLETIRQSHY AAGDQVNQAQ GKLYEASAEV
GRLEAEIRFV VDGRLRVEQR LAQLKEQTAQ WATRQEDAAA ETESLAAQAI EAEEKAELLV
AQTEEHQTQL PALEEALRQA QAKSNEQRTG VAQVQQQIQV LAADQRNIEE QSRTLALRHE
RLTADRNALN APDEARLANL TAQFSGAQEA QAESEARLHE LTETVPQLDE ERRTLQQTVN
TESAKRADLS ARMEALKALQ EKVKTDGKLK PWLEKHGLGS LQGLWSRIHI EQGWENALEA
ALRERLGALE VSRLDMVRGF AGTDGRGDGE GPPAKLSFYT APHAAVPARS NPSVSLKPLA
DLLRLNDAGQ SALLGDWLHG CYTTLNLDEA LAARDKLDAG EVIYVRSGHA VTQHSVSFYA
QDSEQAGLLA RAQEIENLDK QLKAQALISD EARSALVRAE ATYADAAQRL VTARREAAEG
QSRAHELQVE VLRLTQLAEQ TRARSEQIQG DMAEIEAQLG ELEERKVTAE ARFEELDMQL
ADSQERHAQF DDRVIDTERK LGESREQQRT LERQAQEAQF ALRSLASRRE ELARSIAIAT
QQAASIATEE ERAKEELSRL TDAAAQAGLQ SALSVKLERE ADLGAKRSQY DDLTNKLRAS
DERRLQLERE LDPLRQRITE FQLKEQAARL GFEQYEQLLN DAQADLVAVE QSIQAGNVRL
TGLQGEIDRL HREIQSLGAV NLAALDELSA ARERKQFLDA QSADLNEAMG TLEDAIKKID
METRDLLAST FETVNTHFGK MFPELFGGGN ARLVMTGEEI LDAGVQVLAQ PPGKKNQTIH
LLSGGEKALT AIALVFAIFQ LNPAPFCLLD EVDAPLDDAN TERYAKLVSS MSKETQFLFI
SHNKIAMEMA EQLIGVTMQE QGVSRIVAVD MEAALGFSEI AA
//
