ID A0A1B8WJU8_9BACI Unreviewed; 1192 AA.
AC A0A1B8WJU8;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE RecName: Full=Chromosome partition protein Smc {ECO:0000256|HAMAP-Rule:MF_01894};
GN Name=smc {ECO:0000256|HAMAP-Rule:MF_01894};
GN ORFNames=A7975_02810 {ECO:0000313|EMBL:OBZ16851.1};
OS Bacillus sp. FJAT-26390.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=1743142 {ECO:0000313|EMBL:OBZ16851.1, ECO:0000313|Proteomes:UP000092623};
RN [1] {ECO:0000313|EMBL:OBZ16851.1, ECO:0000313|Proteomes:UP000092623}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FJAT-26390 {ECO:0000313|EMBL:OBZ16851.1,
RC ECO:0000313|Proteomes:UP000092623};
RA Liu X., Pan Z., Shi H., Ge C., Che J., Lan J., Chen Z., Chen Q., Liu B.,
RA Zhu Y., Wang J., Liu G.;
RT "Bacillus sp. FJAT-26390.";
RL Submitted (MAY-2016) 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}.
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:OBZ16851.1}.
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DR EMBL; MAQX01000001; OBZ16851.1; -; Genomic_DNA.
DR RefSeq; WP_065384066.1; NZ_MAQX01000001.1.
DR AlphaFoldDB; A0A1B8WJU8; -.
DR Proteomes; UP000092623; 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 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:UP000092623}.
FT DOMAIN 523..642
FT /note="SMC hinge"
FT /evidence="ECO:0000259|SMART:SM00968"
FT COILED 167..201
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 262..366
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 684..883
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 908..949
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; 134941 MW; A95A9F576BE962E0 CRC64;
MFLKRIELSG FKSFADRTEM EFVTGITAVV GPNGSGKSNI SDGIRWVLGE QSAKSLRGGK
MEDIIFAGSD ARKAVNYSEV SLTLDNADGA LPLEYNEVTV TRRVHRSGDS EYLINKQPCR
LKDITELFMD TGIGKEAYSI IGQGRIEEIL STRSEDRRGI FEEASGIVKY KSRKREAQRK
LDETETNLLR IHDLVTELED QVGPLRKQSE KAIHFKALKE QLKTKEISMY VHNIEQIHGT
WTEANGKLER LTQEQLQLST VVSKHDAHLE KDRQQLRELE QALDQLHEAM LQISEDFEKC
EGYGEVLKER KRNLEQNKRQ LEESIASQDA RIGTMTQEEA EFRSRAAALQ LQLADLRSKI
SEEEARLLGV AGGAVADAEE TLKSELLEVL SAMAQHRNEI RYAAQQQDTL QRRMERISED
ETKWLEQQEK LDARRSELAE ALESTLARLE QARSKTLTES EQTRAISQSL EEVTLAIRKW
EQKLDSHVSR RDTMKEMQDA LDGFMQGVKE VLKASRRGNG GISGVHGAVA ELVRVPERIE
TAVETALGGA LQHIVMEDEK TARTAIAFLK QRQLGRATFL PLDVIRGRQV PEHDKRTAES
VEGFVGVAAD LVSSDSRYAA IVNNLLGNVL LAETLEQANR IASKCQYRYR VVTLEGDIVN
AGGSMTGGSL QKKGASLLGR QRQIDGLDQE IADARRMVEQ LRSKLSDLRK EHSIRTHNIE
ELRAEGEKSR IEEQQIRAEL QQLHNEAKHL DEQRQLYSAD RNTHLSEQKD VQAAAAAAEL
RLEQLVLDEV RLQEAIRMAE ERRKASESAK EELQGQLTDI KIAAAKTDQE KLSFEDQSAR
VRADIQRAKQ ELEGLRSLSV QQEEEIERHA NETVQQIEQL NHLRIKKQEC AEQTDLKRSA
RAQRIAELDL GESETKEQRA QLRQVEEQMR QTEIAANRLD VELDNLLRKL SEEYELSYEL
AKEQYPVPED VLGTQNEVRD IKRQITSLGE VNLGAIEEYE RVSERFQFLS EQKDDLIDAK
TTLYQVIREM DEEMSKRFKT TFEAIRGHFV VVFAKLFGGG RADLVLVEPD RVLDTGIDIV
AQPPGKKLQN LQLLSGGERA LTAIALLFAI LQVKPVPFCV LDEVEAALDE ANVSRFAQYL
REFSELTQFI VVTHRKGTME EADVLYGVTM EEGGVSKLVS VRLEDEEEPV SA
//
