ID   A0A1I5E784_9SPHN        Unreviewed;      1128 AA.
AC   A0A1I5E784;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-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=SAMN05428984_2055 {ECO:0000313|EMBL:SFO07173.1};
OS   Sphingomonas sp. OK281.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Sphingomonas.
OX   NCBI_TaxID=1881067 {ECO:0000313|EMBL:SFO07173.1, ECO:0000313|Proteomes:UP000199378};
RN   [1] {ECO:0000313|EMBL:SFO07173.1, ECO:0000313|Proteomes:UP000199378}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OK281 {ECO:0000313|EMBL:SFO07173.1,
RC   ECO:0000313|Proteomes:UP000199378};
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; FOVZ01000002; SFO07173.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1I5E784; -.
DR   STRING; 1881067.SAMN05428984_2055; -.
DR   OrthoDB; 9808768at2; -.
DR   Proteomes; UP000199378; Unassembled WGS sequence.
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:UniProtKB-KW.
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; 1.20.5.340; -; 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; IPR011890; SMC_prok.
DR   PANTHER; PTHR43977; STRUCTURAL MAINTENANCE OF CHROMOSOMES PROTEIN 3; 1.
DR   PANTHER; PTHR43977:SF1; STRUCTURAL MAINTENANCE OF CHROMOSOMES PROTEIN 3; 1.
DR   Pfam; PF02463; SMC_N; 1.
DR   PIRSF; PIRSF005719; SMC; 2.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_01894};
KW   Coiled coil {ECO:0000256|HAMAP-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}.
FT   DOMAIN          3..1111
FT                   /note="RecF/RecN/SMC N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02463"
FT   REGION          443..469
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          167..201
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT   COILED          290..380
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT   COILED          614..662
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT   COMPBIAS        452..468
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         32..39
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
SQ   SEQUENCE   1128 AA;  119757 MW;  5F8E86859984A090 CRC64;
     MQIKRLRITG FKSFVDPADL RIEPGLTGVV GPNGCGKSNL LEALRWTMGE ASAKSLRGAG
     MEDVIFAGTA TRPPRDFAEV SILAEIAGDE REIVRRIERG AGSAYRIDGR DVRAKDVGLL
     FADAATGAHS PALVSQGKIG AVIAAKPADR RAMLEEAAGI AGLHVRRKDA EGKLRATEAN
     LAKLDEIISD QDARAAALKR QARAAERYRL ISAQIRVAEA RTVFARWREA ATAADATKVE
     ATAAETRVRA TTEAERAAAA DQHRAIEAVA TARTAALAAR DLVGDLAHRL AALKTEKASV
     ERRIADLTDA RTRIADDRAR EGSLASDAAA ALARLADEAR ALDTAIADAT AAIPDLDAAL
     AETERSVRDA EVSLAQALAT QARDAAEVRV ASAALAAART RADRANRDAA QIAAALLALG
     DPAPLAAERE TAAETRRAAT AAAESARKAI TQADTDEATA TSARDAAETT RATARADLAA
     IDSEVTALTK ATQRSGRDRL LDHVSANTGY ERALAAALGD DLDTGLDAWA GAKPREDDPA
     APADAEPLAE HVDAPPALAR RLAQVFVVDT DGQQHLAVGQ RIVTRHGQLR RWDGFTATGT
     GAAAAERLVR RNRLAALQAA RPAAAKALDE AERTRAAIDE RIAQARGQSQ TARAALQRAE
     TAARDAIRQE DRAAAALERL ATQRADLDVR AHRIADDVAD AHADLTRAEA AMAAVPDGIA
     NARQVAALQY DAERARAAVA QARADRTTLD RSIATHRERL SAAQADTRSW RARAGEAAKR
     IAAMDTRETT LATDLAAIAA RPAALDAEIE TLDAEHQDAR TTADALLATE RTAETAARTA
     DNAHRAATEA LAVAREARAG AIARVENHEA RRLDLGRLSG ERFQCPAPVL PERLGFAVAD
     VRAPTEESAT HDRLTTDRER IGPVNLVAEI ELAELEDSAL GNAVERDELG QAVNRLRGSI
     GTLNREGRQR LLAAFEAVNG HFQRLFTTLF DGGAAHLELI DSDDPLEAGL EIMAQPPGKR
     LQSLTLLSGG EQALTAVALI FGLFLTNPAP ICVLDEVDAP LDDANIERFC DLLDRMSRDT
     DTRYLVVTHN AVTMSRMHRL FGVTMIERGV SRLVSVDLQA ATGLIAKG
//