ID A0A1X7A7U9_9RHOB Unreviewed; 1151 AA.
AC A0A1X7A7U9;
DT 05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2017, 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 ECO:0000313|EMBL:SLN72838.1};
GN ORFNames=ROA7450_04066 {ECO:0000313|EMBL:SLN72838.1};
OS Roseovarius albus.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Roseovarius.
OX NCBI_TaxID=1247867 {ECO:0000313|EMBL:SLN72838.1, ECO:0000313|Proteomes:UP000193061};
RN [1] {ECO:0000313|EMBL:SLN72838.1, ECO:0000313|Proteomes:UP000193061}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CECT 7450 {ECO:0000313|EMBL:SLN72838.1,
RC ECO:0000313|Proteomes:UP000193061};
RA Afonso C.L., Miller P.J., Scott M.A., Spackman E., Goraichik I.,
RA Dimitrov K.M., Suarez D.L., Swayne D.E.;
RL Submitted (MAR-2017) 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; FWFX01000020; SLN72838.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1X7A7U9; -.
DR OrthoDB; 9808768at2; -.
DR Proteomes; UP000193061; 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 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; 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; PF02463; SMC_N; 1.
DR PIRSF; PIRSF005719; SMC; 2.
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:UP000193061}.
FT DOMAIN 4..1136
FT /note="RecF/RecN/SMC N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02463"
FT REGION 406..436
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 466..485
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 674..742
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 766..828
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 861..888
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 184..218
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 289..334
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 936..991
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COMPBIAS 713..742
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 766..819
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 864..888
FT /note="Basic and acidic 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 1151 AA; 126632 MW; 383A7E234584501C CRC64;
MHFSKLRLTG FKSFVDPTDL IITDGLTGVV GPNGCGKSNL LEALRWVMGE NRPSIMRGGG
MEDVIFAGAA SRPARNFAEV VCHMDNSDRL APAGFNDADH LEVIRRITRD VGSAYKVNGK
DARAKDVQML FADASTGAHS QALVSQGKIT DLINAKPKAR RKILEEAAGI SGLYQRRHEA
ELKLKGAETN LARVDDVIEQ LATQLVQLAR QARQAQRYRA IGEDLRRSEG LLLYRRWKEA
DLARAAADEE LRERITGAAR MEAAAREAAK LRVQAEDALP ALREEEAIAA AVLQRLQVQR
DTLNEQEQNA RTRIETLTSR IEQLSRDIER EASLNRDAGE TIERLEWEAR ELGKAGEGHD
ERLEIASEEA HEAAAVLQQR ETDLGQLTED VARLAARHHS AQRLLDDSRK MLGKSETEST
RAREAAQGAK EAEARAAQEF EIAQQAEEEA QHIAEEAELA LNAAEEARME TQDREVTARA
ERSEAEGELN ALSAEVTALA KLLERDTAEG GQILDRLQVT SGYEKALGAA LADDLRAPEV
SADGPSGWAL LPGYSNAQTL PAGVNALSSY VNVPEVLARR IGQIGLVSGD DGPRLQAELN
PGQRLVSREG DLWRWDGYRA WAEDAPSAAA LRLEQLNRLE ELKQELAHAT ARAEGAQQAH
EALSLMLARQ TEEDRAAREA RRAADAQVTQ ASRTLSRAEA DRNLAASKHE SLGLAVTRHE
EEAMEARKQL SEAEKGQTDL GDLDEARAQV DDVKMTVEAA RITMMSRRSA HDEIRREGES
RTKRSQEVAK EVSGWRHRLE TAEKRSSELA ERKYTTEEEL VEASAAPEEI AAKREELGEQ
IDKSGARRAE AADALSVAES AAREAVAGER DAERNASDAR EARARSEARM EAARETVAVA
AERITEELEL APEALLEQLD VNPDEMPASD QIEADVNRLK RQRDALGAVN LRAEEDAREV
EEEHTTLVNE KNDLEEAIRT LRSGIASLNK EGRERLLTAF EQVNSNFQML YKHLFGGGEA
NLVMVESDDP LDAGLEIMCQ PPGKKLSVLS LLSGGEQTLT VAALIFGVFL ANPAPICVLD
EVDAPLDDAN VGRFCDLLDE MCRRTETRFL IITHHAVTMS RMDRLFGVTM AEKGVSQLVS
VDLKKAEQMV A
//