ID B1XTT8_POLNS Unreviewed; 1152 AA.
AC B1XTT8;
DT 20-MAY-2008, integrated into UniProtKB/TrEMBL.
DT 20-MAY-2008, sequence version 1.
DT 27-MAR-2024, entry version 84.
DE RecName: Full=Chromosome partition protein Smc {ECO:0000256|HAMAP-Rule:MF_01894};
GN Name=smc {ECO:0000256|HAMAP-Rule:MF_01894};
GN OrderedLocusNames=Pnec_0501 {ECO:0000313|EMBL:ACB43765.1};
OS Polynucleobacter necessarius subsp. necessarius (strain STIR1).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Polynucleobacter.
OX NCBI_TaxID=452638 {ECO:0000313|EMBL:ACB43765.1};
RN [1] {ECO:0000313|EMBL:ACB43765.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=STIR1 {ECO:0000313|EMBL:ACB43765.1};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Kim E., Hahn M., Richardson P.;
RT "Complete sequence of Polynucleobacter necessarius STIR1.";
RL Submitted (MAR-2008) 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}.
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DR EMBL; CP001010; ACB43765.1; -; Genomic_DNA.
DR AlphaFoldDB; B1XTT8; -.
DR STRING; 452638.Pnec_0501; -.
DR KEGG; pne:Pnec_0501; -.
DR eggNOG; COG1196; Bacteria.
DR HOGENOM; CLU_001042_2_2_4; -.
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; 1.10.287.1490; -; 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; 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.
DR SUPFAM; SSF57997; Tropomyosin; 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}.
FT DOMAIN 497..606
FT /note="SMC hinge"
FT /evidence="ECO:0000259|SMART:SM00968"
FT REGION 730..775
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 153..197
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 289..390
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 451..478
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COMPBIAS 730..744
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 11..18
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
SQ SEQUENCE 1152 AA; 128148 MW; 764AD9FDE608A461 CRC64;
MPGQLIGVVG PNGCGKSNII DAVRWVLGES RASELRGESM QDVIFNGSGL RKPSGRASVE
LIFDNTEGRA QGQWSAFTEL GIKRVLTRDG NSSYYVNNQV VRRKDIQDIF LGTGMGPRGY
AIIGQGTINR ILEAKPEELR VFLEEAAGVS KYKERRKETA SRLENTVENL TRVEDILREL
DQQLTRLEKQ ATVAERHAEL STQMKSQQQL LWFVRQTEAG KEQERHANGI RDTQVGLEEQ
TAKLRHIEAE LETMRTQQYA LQDKVSQAQG DLYQTNSDVS QVESQILYVQ EARQRLQQQT
QDLQAQLQRW TVQETDAAQA QRTTEHELSL AAEKKQTLLA DLNGLQEQMP SREEAYQNAN
RELNQARDSL ASIEQRLASL GERIRSMSAQ SDELKGCETR LVGEFDGLRR PDAEALQMAI
DRQTIAARKV EEAKHRAVET QQRVPASDEA RNAAQQKIQV ANQDLAQTEA KLTALTALQA
SVQAQGKIGP WLESKGLKES KRLWQELKVE SGWEAALESV LRERLAAVTA KSVQETLALA
NDAPPSRLAI LLTEEITPAH TSAPADFTPL LSRVQSAGAP RLTSVLQEWL DNIYIASSLE
DALHRREKLP AGGAFVTQQG HLVSRVGVQL YAADSEQAGM LARAQEMESL EKQLRAQQLM
QSELKGELDQ CVAKYQAAHQ AAEQARENAE HAVQEAHGFE VERMQLTQAE EQYSQRAAQI
QGELSELRQQ MEQLAQTQEQ SATELLESEE SKRGLQEALQ VAQEKLERST EERDRLRESL
RAAEMAAQEA AFATRSLQQR IADLQRDQST ARTQIMEIQN KHDSATQELE TLSDEEAQDK
LQGLLLARSA REAALANART EQDALLHQLR EADESRMQVE RGLQPMRDKV VDLQLREQAA
RLNFEQFATL LSDAEADLTA LEASFSPDLK VGALQSEVNR LNTEIQALGP VNMAALDELS
SSRERKQFLD AQSADLNEAM QTLTDAIARI DAETRDLLQG TFDQVNAHLG KLFPELFGGG
HAELVMTGEE ILDSGVQVMA QPPGKKNSSI YLLSGGEKAL TAIALVFSLF LLNLTPFCLL
DEVDAPLDDA NTLRYAQLVA KMSDKTQFLF ISHNKITMEI AHQLIGVTMQ EQGVSRIVAV
DISSAVSMVE TA
//
