ID A0A1G9Y198_9BACI Unreviewed; 1189 AA.
AC A0A1G9Y198;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, 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 ORFNames=SAMN05216498_1199 {ECO:0000313|EMBL:SDN02844.1};
OS Tenuibacillus multivorans.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Tenuibacillus.
OX NCBI_TaxID=237069 {ECO:0000313|EMBL:SDN02844.1, ECO:0000313|Proteomes:UP000199334};
RN [1] {ECO:0000313|EMBL:SDN02844.1, ECO:0000313|Proteomes:UP000199334}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.3442 {ECO:0000313|EMBL:SDN02844.1,
RC ECO:0000313|Proteomes:UP000199334};
RA de Groot N.N.;
RL Submitted (OCT-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. {ECO:0000256|HAMAP-
CC Rule:MF_01894}.
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DR EMBL; FNIG01000002; SDN02844.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G9Y198; -.
DR STRING; 237069.SAMN05216498_1199; -.
DR OrthoDB; 9808768at2; -.
DR Proteomes; UP000199334; 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; 1.10.287.1490; -; 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:SF2; STRUCTURAL MAINTENANCE OF CHROMOSOMES PROTEIN; 1.
DR PANTHER; PTHR43977; 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:UP000199334}.
FT DOMAIN 520..639
FT /note="SMC hinge"
FT /evidence="ECO:0000259|SMART:SM00968"
FT REGION 696..727
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 181..475
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 996..1026
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 1189 AA; 137554 MW; A9AFBE45B97575D7 CRC64;
MLLKKLESVG FKSFAERITV DFVSGVTAVV GPNGSGKSNI TDAIRWVLGE QSAKSLRGAK
MEDIIFAGSE TRRALNVAEV TLTLDNKDQR LPIDYEEVAV TRRVYRSGES EYLINKQPCR
LKDIIDLFMD SGLGKEAFSI ISQGKVEEIL SSKSEERRSI FEEAAGVLKY KQRKSKAVKK
LAETDDNLSR VEDIIHEIEG QLEPLKEQAA VAKEYLEKKE ELEQQEVSLI VTEIEHIHTD
WESLLEQIDQ LKEQLMQEKT AIQKDESNVE EIGQQVQALD TKVNQLQEEK LNLTQQIEQL
DGQKNVLVER LKHFDESRDK LTNDIKESQN HIDQYEWDYE DHDKRLQLLE ESRHETKESI
NQIKQEIENS GVDIEEKIES LKAEYIDLLN DQAANRNEKS SIEKQIEQTQ LRKQRLDERF
EQLIEERQSL EKDQELQAKE KVQLDDHIQS IDEDIYKLQS EYEQLFSKIR EDEEKLQKGY
RIIEQLRSKK EMLEDMKDSY SGFFYGVKSL LQAKERGKVS GIHGAVAQLV NIPNDYVTAM
ETALGGQAQH IVVSTDQDAR QSIKWLKQTN NGRATFLPLT TIKSRSIDSN TNQQIKDHSG
FIGVASDLVQ YDNQYHAIVQ NLLGNVIISR TLKDANELAK LSRHRFRIVT LEGDIVNPGG
SMSGGAKKRS NQTSLFTREQ ELKEIKTKLT DYEKKSQQFE QQLNDKKQKS NDLQQTIRSK
QQDKDDFNEK YQMVKEGYQS LQARFSNIND QLAVYDQENS QYNEEINQLK QELETITRKL
EGQDEQADKH KHEIDHLTSN QSNFKETVEK HKERLNHMQI RLAEQESDVR NQKERLEQVQ
GDLNEARGVK TQLEEELQKL EESHQNSKTI DELSQEITDT RTTLTHINDQ LEQNKEKRNN
LAQSREDLER ELKERNRLYE QQSNHLQQLE VKANRLDVDL ENRLNRLSEE YMLTFEKAKA
DYGLTEEIDE ARENVKLIKR SIDELGTVNL GSIEEYERIQ ERHQFLSEQQ EDLLEAKATL
HSIIQEMDDE MIRKFSETFE QIQKQFSIVF KELFGGGRAE LKLTNPDDLL ETGVDIIAQP
PGKKLQNLSL LSGGERALTA IALLFAILRV RPVPFCVLDE VEAALDEANV IRFGKYLKEF
SEHTQFIVIT HRKGTMENAD VLYGITMQES GVSKLVSVKL EETEEMVFN
//
