ID S0EXR6_CHTCT Unreviewed; 1203 AA.
AC S0EXR6;
DT 18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2013, sequence version 1.
DT 27-MAR-2024, entry version 53.
DE RecName: Full=Chromosome partition protein Smc {ECO:0000256|HAMAP-Rule:MF_01894};
GN Name=smc {ECO:0000256|HAMAP-Rule:MF_01894};
GN ORFNames=CCALI_00763 {ECO:0000313|EMBL:CCW34588.1};
OS Chthonomonas calidirosea (strain DSM 23976 / ICMP 18418 / T49).
OC Bacteria; Armatimonadota; Chthonomonadetes; Chthonomonadales;
OC Chthonomonadaceae; Chthonomonas.
OX NCBI_TaxID=1303518 {ECO:0000313|EMBL:CCW34588.1, ECO:0000313|Proteomes:UP000014227};
RN [1] {ECO:0000313|Proteomes:UP000014227}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 23976 / ICMP 18418 / T49
RC {ECO:0000313|Proteomes:UP000014227};
RA Lee K.C.Y., Morgan X.C., Dunfield P.F., Tamas I., Houghton K.M.,
RA Vyssotski M., Ryan J.L.J., Lagutin K., McDonald I.R., Stott M.B.;
RT "Genome sequence of Chthonomonas calidirosea, the first sequenced genome
RT from the Armatimonadetes phylum (formally candidate division OP10).";
RL Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
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; HF951689; CCW34588.1; -; Genomic_DNA.
DR RefSeq; WP_016482148.1; NC_021487.1.
DR AlphaFoldDB; S0EXR6; -.
DR STRING; 454171.CP488_00388; -.
DR KEGG; ccz:CCALI_00763; -.
DR PATRIC; fig|1303518.3.peg.772; -.
DR eggNOG; COG1196; Bacteria.
DR HOGENOM; CLU_001042_2_2_0; -.
DR InParanoid; S0EXR6; -.
DR OrthoDB; 9808768at2; -.
DR Proteomes; UP000014227; 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; 1.20.1060.20; -; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000014227}.
FT DOMAIN 523..638
FT /note="SMC hinge"
FT /evidence="ECO:0000259|SMART:SM00968"
FT COILED 167..208
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 255..443
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 680..777
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 806..889
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 918..945
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 1203 AA; 136065 MW; FD209FBD5DB92EFE CRC64;
MQLKQLQLLG FKTFADRIEL QIGPGLTAIV GPNGSGKSNI VDAILWVLGE QNPRLLRAER
AQDVIFSGSD KRKPLGMAEV RLLLDNSDHF LPISFSEVSI SRRIYRSGES QYFINGAPCR
MKDIVELFLD TGAGKGAYAV VGQQEVDAVL SARPEDRREL FEEAAGIKKY RVKKREALRK
LEAAEANLQR VRDILRELEA QKEPLERQVI AARRYLGYQE RLREIEVGLL VAEAKQADYE
LYGIRQEQEL DRAELHRIEI QQAQFEQHLA ELTEQVVQVE ENLEIARTNH QNLLSMAERL
QSRMAVLEER ARAAVRTKEQ ALQEIAELNT QKELLENLIA SEAEESARLQ AELAEREQAW
AAEQAALQAV EQAVAEILRE LEAQRSQQLR RAEERAGRLA ALDGVKARLD ETRQQLDALL
KEATLLQEQR LQAEERLRQL TVEQAQRRAQ RDELYQTQEH LETQQKGLQA EADACRNRWE
AARRAYSEQA ARLSTLIELQ ESYEGFYYGV RALLQAARAG AVRGDYRPVV DLLTVPKPYR
IAIEVALGSS LQDIVTPSAE EAKAGIAWLK QHRAGRVTFL PLTLLRPGRP LDPLPAEEGI
EGVAVNLVGF DNRYVPAIQL LLGRVVVVRN LDTAITLSRR LSGWSRMVTL EGELLTPGGA
LTGGSLQGLG AHLVGRKGEI DDLKTRLPDL QAEVDRLATQ HKELLQKQQE TAKEHANLMQ
ELANLDQAIA IAAGTQAAAE RELARLQRQE VEHQQAQQLL KTRIGELEKE QERLENLILS
RHEDDTDAEN ALIALQKEVE IRIAKRDALR SNAARLEVET TELRTQLQGL KRSQQENRQA
LEELQRRIEQ RKSLHAQIQQ EEAKVAEETT RLAEQRQQIL RQLQEAEKSV QQCLTSRQQK
LDAHTKTNEA LREATQRHRE ITVRLHETEL RIARLEMQLS QAAERLLQEY NLPIEQALCY
QETVALDENT VREVARLRRE IRAMGHVNTG AIEEFERLTE RCDFLTTQQA DLEKSRAGLL
DTISEIDAST RDIFLQTFEA VREEFDRLFK RLFGGGRAQL LLTNPNDLLE TGIEIIAQPP
GKKAQNLSLL SGGERALTAI ALLFAFLSVR PSPFVILDEV DAPLDGANVE KFVQLVREFS
ERSQFLVITH NPVTMEAAPI WYGVTMREPG VSSIISYRVP QLKESDPTQL SEVGSPNGEK
TFS
//
