ID A0A2A5YJ91_9PROT Unreviewed; 1132 AA.
AC A0A2A5YJ91;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 24-JAN-2024, entry version 21.
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:PDH64562.1};
GN ORFNames=CNE92_02060 {ECO:0000313|EMBL:PDH64562.1};
OS SAR116 cluster bacterium MED-G05.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; SAR116 cluster.
OX NCBI_TaxID=1986234 {ECO:0000313|EMBL:PDH64562.1, ECO:0000313|Proteomes:UP000219577};
RN [1] {ECO:0000313|EMBL:PDH64562.1, ECO:0000313|Proteomes:UP000219577}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MED-G05 {ECO:0000313|EMBL:PDH64562.1};
RA Haro-Moreno J.M., Lopez-Perez M., De La Torre J., Picazo A., Camacho A.,
RA Rodriguez-Valera F.;
RT "Fine stratification of microbial communities through a metagenomic profile
RT of the photic zone.";
RL Submitted (AUG-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}.
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:PDH64562.1}.
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DR EMBL; NTKW01000005; PDH64562.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2A5YJ91; -.
DR Proteomes; UP000219577; 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: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; 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 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.
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 2..1113
FT /note="RecF/RecN/SMC N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02463"
FT REGION 634..690
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 163..204
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 289..316
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 775..851
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 927..968
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COMPBIAS 635..676
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 25..32
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
SQ SEQUENCE 1132 AA; 121899 MW; 639F0224E18DB493 CRC64;
MAGFKSFAES AEVDIETGLT GIVGPNGCGK SNIVEGLRWV MGESNARQMR GGEMDDVIFA
GTDTRPARNL AEITLLLDNS DRSAPSEFNN DDDLEITRKI ERGKGSSYFV NTRPARAKDV
QLLFADSATG ARSSGIVSQG RIGAIVGARP TDRRALLEEA ANIRGLHARR HEAELRLKGA
ETNLERLDDV VAGLIEQRDS LKKQARQAAR YRSVADRIRK AEAQLLLARW HAAEQALADA
AETLRTLQLT TAEHTQIAAS QATTRAELAA KLPPLRETEV ARAAEYQRLA ISRDELDREE
ARIRDALERA KDQQHRITED IEREASLRTD ASSAIDRLTA ETAGLRTTID EAAPQQESAA
SELATIRAEQ DIADSALADA AGRVRAAEST RTALSGRITD LRSRQDAARA ALDAISLAEL
QQAAGTAHSD LEAAEARNAA DVARLTQAES VLADAQNAAE SAATIYRESD TRTTRLQAEI
DALGYLLAAG DGSGDVPIAD SLTVLDSMEQ ALTACLSEEL SAPAGSGDVS YWRSAGAQHD
LEPPEGTRPL ADSVIGAPEL ASTLAGIGVV DTPGQAQFLQ DSLRPGQSVT TQQGGLWRWD
GFVRRPGAQD SGAERIRQRQ RLETLEAELA KAATEQNRLS ASASTADQAL AEARTSQTGA
RADAAESNTS LSTARRAEES TKLRLSAAEE RADELRTTAA TLGDDLASAE AEAAALGDDA
ALQKGEADAR QVAEAVRTRV AEAMQAESRF AEAVRVASDR LASAATETEA WQKRLVGAEN
RVGEMKTRLA EGEAEIERLS AMPDALAKQR DALADTLQTA ETVRQQAADD LRRAETELAA
AETAQREADT TLATSREQLV RAEGTRDFAT ETRRVVEEQI SDKLDCSPDG LASIADIEDA
TSLPEVTVLE DRVHRLIRER DTIGPVNLRA ETEMEEVAAR IESIEAEQED LVAAIEKLRA
AISRLNRQGR EQLLNSFAAV NNHFKDLFKV LFGGGTAELQ LTESADPLEA GLEILAQPPG
KRLQSLSLLS GGEQALTALA IIFAVFLTNP APICVLDEVD APLDDTNVAR FCDLLRDIAG
KTDTRFMVIT HHRMTMARMD RLFGVTMEQR GISKLVSVDL QTAERIRDAA VA
//
