ID A0A0M2GYL8_9MICO Unreviewed; 1172 AA.
AC A0A0M2GYL8;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 30.
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:KJL38927.1};
GN ORFNames=RS81_02336 {ECO:0000313|EMBL:KJL38927.1};
OS Microbacterium ketosireducens.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Microbacterium.
OX NCBI_TaxID=92835 {ECO:0000313|EMBL:KJL38927.1, ECO:0000313|Proteomes:UP000033956};
RN [1] {ECO:0000313|EMBL:KJL38927.1, ECO:0000313|Proteomes:UP000033956}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 12510 {ECO:0000313|EMBL:KJL38927.1,
RC ECO:0000313|Proteomes:UP000033956};
RA Corretto E.;
RT "Draft genome sequences of ten Microbacterium spp. with emphasis on heavy
RT metal contaminated environments.";
RL Submitted (FEB-2015) 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:KJL38927.1}.
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DR EMBL; JYIZ01000053; KJL38927.1; -; Genomic_DNA.
DR RefSeq; WP_045276256.1; NZ_JYIZ01000053.1.
DR AlphaFoldDB; A0A0M2GYL8; -.
DR STRING; 92835.RS81_02336; -.
DR PATRIC; fig|92835.4.peg.2370; -.
DR OrthoDB; 9808768at2; -.
DR Proteomes; UP000033956; 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; 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|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW 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|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_01894}; Reference proteome {ECO:0000313|Proteomes:UP000033956}.
FT DOMAIN 506..613
FT /note="SMC hinge"
FT /evidence="ECO:0000259|SMART:SM00968"
FT COILED 167..201
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 345..372
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 401..483
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 727..754
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 792..826
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 954..1016
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 1172 AA; 125609 MW; 9F642835F1E2F560 CRC64;
MHLKSLTLKG FKSFAQPTTF ALEPGVTCIV GPNGSGKSNV VDALAWVMGE QGAKTLRGGK
MEDVIFAGTA TRGPLGRAEV QLTIDNSDGA LPIEYSEVSI SRTLFRNGSS EYAINGETCR
LLDVQELLSD SGLGREMHVI VGQGRLDAVL QATPEDRRGF IEEAAGILKH RRRKEKTLRK
LEAMEANLMR LSDLAGELRR QLKPLGRQAE IAREAATIAA VVRDAKARLL ADELVALRTE
LADHARNEQE RHTERLVLQD QLDNVRARVE QLENDQRSEV VDDARRTAFG LERVQERVRS
LYSLAGQRLA LLAESDADER LELTTVSQAM IDEARGEIDE ISDGLGEMQD AAAEASREVI
RARAELDALD SDIAAQSALV SEHDMKLTAL RGSAEAADSA LAAVRAAVER QQRALDAALA
RRAETEETLR GVDPDLVPEG TSAEHAAAYE RAQREATDAE SSVGSLRERL HAAEREREAL
TAQTSALGRA LEVKNAAAEI VAQGALGVRG LIGDAIKVTA GYESAIAAAL GPLAEGVLVG
SRDEAYAIAA SAREGDLGVV DIAIADAGAM RPRQSPPAGV VAAQDVVTAP EGVLGILAFV
FIADDLDAAA AAGPALAAAD LGGPVTVVTR AGEVVTEYTV RAGSGEGRSR LELAAERDGA
AERRDEIIVV ADSLREALTD ATTALEGARR RTKDALTALR EHDAALAAHT EQVNRATVRH
EAAVAECDRL AAGLAQAESA VEDAEAAARS AGDQLTTALE APRPILDASA RDGMLAALEE
ARDGEMRSRL DVETLRERIR AGEARVAGLM RQREREKEAA AEAARRAVVR RAQRDIAAGV
SSQLPALLDS IDRSVSQARV DLAAAESARI ALTEELGALR TTESSLRERL AGLTESVHGI
ELQIHEKRLH VTGLLERVAS ELGLDENILV SEYGPDQAVP ADVGGDDATV PYERSAQRRR
LQEAERKLTQ LGRVNPLALE EFAALEQRHK FMTEQLADLT QTRTDLLTII EELDERMQVI
FLAAFEDTKV AFGEVFPILF PGGTGSISLT DPESPLTTGI EVAVRPVGKK IERLSLLSGG
ERSLAAVALL TAIFKARPSP FYILDEVEAA LDDANLGRLL GVFEQLRESS QLIVITHQKR
TMEIADALYG VSMRQDGVSA VVGQRVGERV AS
//
