ID C0QSN8_PERMH Unreviewed; 1162 AA.
AC C0QSN8;
DT 05-MAY-2009, integrated into UniProtKB/TrEMBL.
DT 05-MAY-2009, sequence version 1.
DT 24-JAN-2024, entry version 75.
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:ACO03931.1};
GN OrderedLocusNames=PERMA_1923 {ECO:0000313|EMBL:ACO03931.1};
OS Persephonella marina (strain DSM 14350 / EX-H1).
OC Bacteria; Aquificota; Aquificae; Aquificales; Hydrogenothermaceae;
OC Persephonella.
OX NCBI_TaxID=123214 {ECO:0000313|EMBL:ACO03931.1, ECO:0000313|Proteomes:UP000001366};
RN [1] {ECO:0000313|EMBL:ACO03931.1, ECO:0000313|Proteomes:UP000001366}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 14350 / EX-H1 {ECO:0000313|Proteomes:UP000001366};
RX PubMed=19136599; DOI=10.1128/JB.01645-08;
RA Reysenbach A.L., Hamamura N., Podar M., Griffiths E., Ferreira S.,
RA Hochstein R., Heidelberg J., Johnson J., Mead D., Pohorille A.,
RA Sarmiento M., Schweighofer K., Seshadri R., Voytek M.A.;
RT "Complete and draft genome sequences of six members of the Aquificales.";
RL J. Bacteriol. 191:1992-1993(2009).
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; CP001230; ACO03931.1; -; Genomic_DNA.
DR RefSeq; WP_012676170.1; NC_012440.1.
DR AlphaFoldDB; C0QSN8; -.
DR STRING; 123214.PERMA_1923; -.
DR PaxDb; 123214-PERMA_1923; -.
DR KEGG; pmx:PERMA_1923; -.
DR eggNOG; COG1196; Bacteria.
DR HOGENOM; CLU_001042_2_2_0; -.
DR OMA; HNKIAME; -.
DR OrthoDB; 9808768at2; -.
DR Proteomes; UP000001366; 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 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; TIGR02169; SMC_prok_A; 1.
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; 2.
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:UP000001366}.
FT DOMAIN 517..632
FT /note="SMC hinge"
FT /evidence="ECO:0000259|SMART:SM00968"
FT COILED 168..493
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 666..696
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 722..1016
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT BINDING 36..43
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
SQ SEQUENCE 1162 AA; 135132 MW; 1FC4BCCC714E1E51 CRC64;
MSKAYIDRIH VYGFKSYGLR KLTIPVGNGF VGIVGPNGSG KSNIGDSIVF ALGLATAKSM
RALKLSDLIF SSRGRSAEYA EVEVVFKNEG AFPLNDEEVS IYRKVEHNGK STYRINGRPA
KQYEVEELLS YAGIPKQGYN IVTQGDIFRF VKMTPSERRD LLSEIAGITE YEEKKEKALK
DLTETEEKIQ SAKLVLKEVK IQLKRLEEER ENALLAAQLE EKIEKIQKNI KGVKLYFLLT
EQKKAVDDLK EIEERINRLY EEKEISVQKQ KEQISVIKEL EDRLNRLQES LLPLKEKEGS
ITAQIRTSSD KKSEIEKEIQ SIKENLKELA REKEEKIKEV LSLEEQIKEL KRKLPEIKKE
LEKAEAVLEE KNRKLKEIEI GGSRAKLDLG EVEKEEKSLK DRQSSLQKEK IHIEMEINRI
LEKIEEYHNE IRSLSEEVET LRKSSSNIKS FTESQERKLK SLKSELSRLK LRKETLEKKL
KENREKREKN FQRLAEVLAQ LSQMREDRVI TLIKDINGVY GQVADLIGIK DPELSKAIEV
AGGGRLKNIV VEDDRVAQEC IRVLKENKAG RATFIPLNRI RVSHPAKPPY MRGVIGLAVD
FIDYDKKIEK AVRFVFGDTV IVQDFDSARN LGIGTFRMVT VDGDIFEKSG TISGGFDKNR
GGILGRGSLE QEKIKLEQED ERLKAEEGMM EEELKKIAVK WQETEKELYK LQNETESVIE
RKREIETKID QNLSRINILE EEIINLKKRQ FEQENRLERT EKELSELERN ISYIHKKKED
ILQRMESEGL HQLRKEWEEA TKNVYSLREK KNEIENEIEK LTDRLENNLK VRIFQIENDR
MKLEDSLKIK NRQIEELKNR IEEYSRELSD LWKDLKDREK ERDELIEEIE ERKEELKSLR
YEEENINKEI TYLLEDKGKL EQKVEDLKDE IEILKEEYEG EPVEGDLKVL EKELKELQEK
RQSIGAVNQK ALEDYDQIKE RFDDLSQKLK VLIEEKKSIE EMIESLEEKK IKAFMEVYEA
VNKNLGKIFR RLSPGGKAYL EIENEDDPLS GGILLKARPR GKDVKRLEIM SGGEKTLTAL
AFLFAVQQYR PAPFYYFDEV DAHLDDANAR KIAELMKELS QEAQFIVVTL RDTMASYADR
LLGVSAREGI SDVYSLELAE VL
//