ID A0A101I1Z5_9BACT Unreviewed; 1137 AA.
AC A0A101I1Z5;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=Chromosome partition protein Smc {ECO:0000256|HAMAP-Rule:MF_01894};
GN Name=smc {ECO:0000256|HAMAP-Rule:MF_01894};
GN ORFNames=XE01_0788 {ECO:0000313|EMBL:KUK87316.1};
OS Synergistales bacterium 58_81.
OC Bacteria; Synergistota; Synergistia; Synergistales.
OX NCBI_TaxID=1635274 {ECO:0000313|EMBL:KUK87316.1, ECO:0000313|Proteomes:UP000054873};
RN [1] {ECO:0000313|Proteomes:UP000054873}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=26787827; DOI=10.1128/mbio.01669-15;
RA Hu P., Tom L., Singh A., Thomas B.C., Baker B.J., Piceno Y.M.,
RA Andersen G.L., Banfield J.F.;
RT "Genome-Resolved Metagenomic Analysis Reveals Roles for Candidate Phyla and
RT Other Microbial Community Members in Biogeochemical Transformations in Oil
RT Reservoirs.";
RL MBio 7:e01669-15(2015).
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KUK87316.1}.
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DR EMBL; LGGV01000031; KUK87316.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A101I1Z5; -.
DR STRING; 1635274.XE01_0788; -.
DR PATRIC; fig|1635274.3.peg.51; -.
DR Proteomes; UP000054873; Unassembled WGS sequence.
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 Gene3D; 1.10.287.1490; -; 1.
DR Gene3D; 1.20.1060.20; -; 1.
DR Gene3D; 3.30.70.1620; -; 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; IPR036277; SMC_hinge_sf.
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 SMART; SM00968; SMC_hinge; 1.
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}.
FT DOMAIN 501..617
FT /note="SMC hinge"
FT /evidence="ECO:0000259|SMART:SM00968"
FT COILED 160..218
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 325..478
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 650..715
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 869..903
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 1137 AA; 128815 MW; D63D346825721E4E CRC64;
MYIGRIHLKG FKSFGGSHEI ALSSNFTAVV GPNGSGKSNI LDALRWVLGD GNPSRLRIVR
QGDLLFQGSI SLPPASSSEV MVHLREGNRV STLRRRFTND DGSTMFIDGR RIRLIDLDDI
KRKWRLEGDR FAFISQGEVS EVIQQRPLQR RMHLEAIFGI DLYRKQREEA IQRLDVATLE
MQRILTLKTE LQTRKEAIAD LVIRAREAKG VIDQLEREKS QLYWVKRARS EKILDGIRRE
LSDLGVQATA SKFWTSGWRR ALNRAEDAIN SISEDRGSMA STVTGLERSL MDSRRKLFSL
STSLVGSMER RKALLGDIAG EKDRFAGTAK RMEDLERDVA RAAEEENESS RSFNDARGEW
EQYRKRVEER SDRIRSLREE RAACEAALES ARSRGKGLGL SILEVLGEIS RSEESVKEAR
QDLGRLQEEI EQKRSLEEAA GNRQRDVYAA FQQAAASLQK LSREMSALEG EMETLRETAF
TRVYPAPVQH LLAAVRLGRI DASPRPLADV ISCPDRLVTA LESFLGARQF LLFVKDIDEA
GRCIAHLKAR SAGRATFLPL ESARARHPMR SIKEDRPGIV GWVSDLIGME SEWKECVLHV
LGDLLIVESF DVARDLVREG FRGPAVTLEG DVFQPGGTIS GGKTNKGAGA IEIRRNLQEK
EKEAERLKNE RSRLEEEIAE LEKEERDASE KLRILSEERR ALEDERRSAE AAEAVAARTR
ALADERREGI LAALSSCGRE YLEIRSRLEE LRESSSEEPE SSRELELVKS LEESRSRAEV
AAERLETARR MFTMVQDEYR RSSSRLEELE KGLEDLALAE KSWKRGLAEE GRTYYGIWLR
LQEAMSGMKD LVEGHSRTLT SRERILERSA SATARMESLD SRIRQARQRL DSTEAEIAES
IDMWEERFPY PGEENIDTRD YDRIRRSVRE LEKSLREIGD VDLGVLSEDA SLAERLGFLE
EQLRDVSTGI DELRRLIEET DRQAGTLFST SLKEIDRKFC DLFQRLFGGG EAHLRLSDDD
NLWEAGVEVI ARPPGKRPQH LAQLSGGEQS LSAISLLFAA MEVAGVPLAV LDEVDASLDE
VNLRRFSELA KEYSRAMQLI CMTHRRATME RADLMYGVTM SEPGLSQVVG VRVEDWE
//
