ID A0A2S1GZ17_9BACI Unreviewed; 1192 AA.
AC A0A2S1GZ17;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 24-JAN-2024, entry version 22.
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:AWE06646.1};
GN ORFNames=DCE79_04235 {ECO:0000313|EMBL:AWE06646.1};
OS Lysinibacillus sp. 2017.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Lysinibacillus.
OX NCBI_TaxID=2169540 {ECO:0000313|EMBL:AWE06646.1, ECO:0000313|Proteomes:UP000244315};
RN [1] {ECO:0000313|Proteomes:UP000244315}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2017 {ECO:0000313|Proteomes:UP000244315};
RA Li J.;
RL Submitted (APR-2018) 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; CP029002; AWE06646.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2S1GZ17; -.
DR KEGG; lyz:DCE79_04235; -.
DR Proteomes; UP000244315; 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; 1.20.1060.20; -; 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:UP000244315}.
FT DOMAIN 520..639
FT /note="SMC hinge"
FT /evidence="ECO:0000259|SMART:SM00968"
FT COILED 283..398
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 680..728
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 764..861
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 995..1025
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 1192 AA; 134817 MW; 5ACC9CC36B9CFC6C CRC64;
MFLKRLEVVG FKSFAERVGI DFVPGVTAVV GPNGSGKSNV TDAIRWVLGE QSAKSLRGAK
MEDVIFAGSE SRKPLNFAEV TLVLDNEDER VAIPYTEVSV TRRVYRSGDS EYLLNNQQCR
LKDITDLFMD SGLGKEAFSI ISQGRVDEIL NSRPDDRRSI FEEAAGVLKY KLRKKKAEHK
LVETDENLNR VLDILHEIEV RLEPLKIQAS SAKDYVRMTE ELKDFDIALM VHDLLAHEKT
LQKFEAEHKE LSTSEKKHAA EITNLEQSVR KIRTDLKAID GVLDASQEQL VEASAEVERW
EGRRALFNEK RSNAEKQTQQ LKLNLQQATQ SVNELELEQQ EKRQQFTEKQ KVVQEIRSSL
KQIEQALTRS ASEIEQEIED AKNTYINLLN EEATVKNELK HIDQQLSQEQ ASVERMTGRS
SEMQKELTTV LTSKEVTEQA LQQAELALQD QLGRFDVVQM QLKSSTADLD EKQDLLYKAY
QHHQQLKARK ETLAELEADF SGFFHGVKEI LLARDRKELE GIEGAVAELI QVDAKYSQAI
ETALGAASQH IVTDNEQHAQ RAIGWLKQKR AGRATFLPKT VMRSRKIQHQ QLMDISSHPA
YVALAYELVQ YAPENQTIIE NLLGNVLVAQ NLEGASQIAR LCGFKYRVVT LEGDIVNAGG
SLTGGALKQQ SSLFSRKAEL DKLVTTLADM EATIQKAEKT VAVKKEEIVQ LRHSLEELKL
QGESLREQEQ VHRSKALELD MTAKSLKTTV SITQSEQSSL STRKESLAEQ QQVAHKRLEE
LRTELQDIQQ TVDELTLAKT QSETQKDVLR EQLAQKRSEL AVAQEQLTQV QAAIAGIELN
LTKAQNLVEK ISQEIEWVES EDGLNGPSSE ELAQTILDWS TKKDALNETI QKNRASRTVL
HEQMTEAEIQ LQEVQRVHKS YMDALRTLEI KRSRIDFEMN SMQQQLLEQY ELDVLTAQEE
AIGIEDEEQV RRKVKLLKQS IEELGPVNLN AIEEFDRVQE RYAFLSEQRE DLVEAKDTLH
KAIGEMDEEM TERFNDTFKQ IRQQFSVSFR ELFGGGAADL VLLDPENLLE TGIEIIAQPP
GKKLQNLSLL SGGERALTAI ALLFAILNTR PVPFCILDEV EAALDESNVA RYSDYLRKFS
EDTQFIVITH RKGTMEGADV LYGITMQESG VSKLVSVKLE EQSELVGQGS GK
//
