ID A4IM68_GEOTN Unreviewed; 1187 AA.
AC A4IM68;
DT 01-MAY-2007, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2007, sequence version 1.
DT 24-JAN-2024, entry version 97.
DE RecName: Full=Chromosome partition protein Smc {ECO:0000256|HAMAP-Rule:MF_01894};
GN Name=smc {ECO:0000256|HAMAP-Rule:MF_01894,
GN ECO:0000313|EMBL:ABO66422.1};
GN OrderedLocusNames=GTNG_1046 {ECO:0000313|EMBL:ABO66422.1};
OS Geobacillus thermodenitrificans (strain NG80-2).
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Geobacillus.
OX NCBI_TaxID=420246 {ECO:0000313|EMBL:ABO66422.1, ECO:0000313|Proteomes:UP000001578};
RN [1] {ECO:0000313|EMBL:ABO66422.1, ECO:0000313|Proteomes:UP000001578}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NG80-2 {ECO:0000313|EMBL:ABO66422.1,
RC ECO:0000313|Proteomes:UP000001578};
RX PubMed=17372208; DOI=10.1073/pnas.0609650104;
RA Feng L., Wang W., Cheng J., Ren Y., Zhao G., Gao C., Tang Y., Liu X.,
RA Han W., Peng X., Liu R., Wang L.;
RT "Genome and proteome of long-chain alkane degrading Geobacillus
RT thermodenitrificans NG80-2 isolated from a deep-subsurface oil reservoir.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:5602-5607(2007).
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; CP000557; ABO66422.1; -; Genomic_DNA.
DR RefSeq; WP_011887122.1; NC_009328.1.
DR AlphaFoldDB; A4IM68; -.
DR KEGG; gtn:GTNG_1046; -.
DR eggNOG; COG1196; Bacteria.
DR HOGENOM; CLU_001042_2_2_9; -.
DR OMA; HNKIAME; -.
DR Proteomes; UP000001578; 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; 2.
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 518..637
FT /note="SMC hinge"
FT /evidence="ECO:0000259|SMART:SM00968"
FT COILED 167..201
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 234..489
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 679..944
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 994..1031
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 1187 AA; 135491 MW; F20679334BB0F508 CRC64;
MFLKRLDVIG FKSFADRVSI DFVPGVTAVV GPNGSGKSNI TDAIRWVLGE QSVKSLRGAK
MEDVIFAGSD SRKPLNVAEV TITLDNEDGF LPLEYQEVSV TRRVYRSGES EFFINRQPCR
LKDIVDLFLD SGLGKEAFSI IGQGRVEEIL SSKPEERRTI FEEAAGVLKY KLRKKKAETK
LAETQDNLQR VNDILHELGQ QLEPLRMQAS IAKEYLEKRE ELERFEVALM VHDIEQLHRQ
WSELNEALNE HQQEEGRLAA ELQKTEAHIE QLRDQITAID ESVDGLQQVL LLASEELEKL
EGRKEVLKER KKHASQRIEQ LDETVIALTE KRRRLTEQLR SEKAALTQLE AGAAALEKEL
KEQQALLSAH EVDIEEEIER RKGDYIDLVH EQAVLKNERL HVEQAIHKLR AKQAALNEAN
SDHLKQRNQL EQQRAALLAE LSRLEQAITE ASSKLAALES ALKEQQVELE QKETSLHQAR
QYRQQAKARQ QWLEEMQHEY AGFFQGVKEV LKARNRLPGI RGAIVELIRV PDRYEIAIET
ALGGAMQHIV VDSEQAARQA IHFLKTNGYG RATFLPLDVI QARSLSERER AAISGHPAFV
GIASELIEYD DIYAAAIAHL LGHVIVTADL KGANELAKLL HYRYRLVTLD GDVVSPGGAM
TGGGAAKKTA SLLGRNRELE TIAAKLREMD DVIARLERDM AAKRRERAEW EAEAAMLKEE
IARLQQSLQE EKEEQRELEW QKKRIDERLA LYDEEKANDE REIAELNNRL GAIDGQLQQL
AEKLQAIDED INRLQVQKQT EQTTKEALQV AITEKKIALA ETKERVKHAR RKAEEIEAEL
AETARGLQQA ERERAALQAE MEAPEWNEEE LEQLRQQKLE DKQKTLELIT SRREQRLDCQ
RRLEHLEQEW KEAKRQHKQL VEVVKDEEVK LNRLDVELAN LLSRLSEEYG LSFEAARSGY
PLEIGADEAR KRVKLIKRAI EELGTVNLGA IDEYERVSER HRFLSEQKAD LEEAKATLHQ
VIEEMDEEMK KRFFTTFEQI RAHFSEVFRE LFGGGRADLR LTDPNNLLET GVDIVAQPPG
KKLQHLSLLS GGERALTAIA LLFSILKVRP VPFCVLDEVE AALDEANVQR YAQYLKRFSR
DTQFIVITHR KGTMEEADVL YGVTMQESGV SKLVSVRLED SKQLVQS
//