ID I9WF72_9SPHN Unreviewed; 1145 AA.
AC I9WF72;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2012, sequence version 1.
DT 24-JAN-2024, entry version 49.
DE RecName: Full=Chromosome partition protein Smc {ECO:0000256|HAMAP-Rule:MF_01894};
GN Name=smc {ECO:0000256|HAMAP-Rule:MF_01894};
GN ORFNames=WSK_2409 {ECO:0000313|EMBL:EIZ78866.1};
OS Novosphingobium sp. Rr 2-17.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Novosphingobium.
OX NCBI_TaxID=555793 {ECO:0000313|EMBL:EIZ78866.1, ECO:0000313|Proteomes:UP000004732};
RN [1] {ECO:0000313|EMBL:EIZ78866.1, ECO:0000313|Proteomes:UP000004732}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RR2-17 {ECO:0000313|Proteomes:UP000004732};
RX PubMed=22933764; DOI=10.1128/JB.01159-12;
RA Gan H.M., Chew T.H., Hudson A.O., Savka M.A.;
RT "Genome Sequence of Novosphingobium sp. Strain Rr 2-17, a Nopaline Crown
RT Gall-Associated Bacterium Isolated from Vitis vinifera L. Grapevine.";
RL J. Bacteriol. 194:5137-5138(2012).
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:EIZ78866.1}.
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DR EMBL; AKFJ01000084; EIZ78866.1; -; Genomic_DNA.
DR RefSeq; WP_008995341.1; NZ_AKFJ01000084.1.
DR AlphaFoldDB; I9WF72; -.
DR PATRIC; fig|555793.3.peg.2356; -.
DR eggNOG; COG1196; Bacteria.
DR OrthoDB; 9808768at2; -.
DR Proteomes; UP000004732; 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 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000004732}.
FT DOMAIN 3..1128
FT /note="RecF/RecN/SMC N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02463"
FT REGION 277..305
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 689..728
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 166..260
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 791..860
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COMPBIAS 278..293
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 689..705
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 1145 AA; 122331 MW; E0ADE7F8035DF50E CRC64;
MRIRRLKLSG FKSFVEPAEL RIEPGLTGVV GPNGCGKSNL LEAIRWVMGE SSPKSMRSGG
MEDVIFAGTA NRPPRAFAEV VLHAETSPRA DGSREDLEVI RRIERGAGSA YRINGRDVRA
KDVALVFADA ATGAHSPALV SQGRIAGVIA AKPAERRAML EEAAGIAGLH VRRKDAEQKL
RATETNLARL EDIMAGLDKH VMALRRQAKA AERYKALSDQ VRLAEARLVF ARWRDAAAAA
EAAKKEARAA EERVTAAQGT ATAAQAAQAA AAQGLADARD ELADRRDDAS AHGHRMATLS
GQLEAAEQRL KDLDRQRNRL DEDRRDADRL TREAAEALAR LERELQDGEQ RLAEDEAQRP
RLAQVLDNAE RAARKAELDL AQATAEQAGV EAEWRIAEAE LTQARARLAR LDQERERLAG
QLAALPEAAS LETAITQARH AAQAAGERLA QARAALEEQQ VRKVQLQAER DEAASALAGA
RGDLTGIERE HTALLRDREA RAKGAKAAHG LPVAIDAVRA APGYERALAA VLGRDAKAPL
GAVPGAEGRF WTGADAPQPV ADSLAAHITA CPPQLAARLA LVHVVDADDE RALAPGEWLV
TRGGVLRRWD GFIARGEGAA EAARLEAENR FTELDAQLPP LREAVSTAQT RHDAAQQALS
GLTAAKIAAE RAIAGAADAE RAALRALDQA EGTRERHRGR RAELDAAAAD LSSQREGAER
DLGTAEASRA ALPDPATGRA GLQMAQALHA GARAALQSAT AALAAHDQGL AVLRERTATQ
RADMRNWQAR AGDATNRLAQ MAGRIDEIES ERAVIAAKPE ALIAQIEQGE TVRTRLAAEL
AQAEAAAAAA AEAARQADAA LAAAQEALAA AREGRAGAAA RAENEDARRV EMTRLSGERF
QCPPPVLPER FAFASAQVGA AQDETATMER LVAERERIGP VNLVAADELA EAEAQLGSNL
TEKAELAEAV NRLRGSIGNL NREGRERLRA AFEAVDGHFR RLFTQLFQGG QAHLALVDSD
DPLEAGLEIY AQPPGKRLQS LTLLSGGEQA LTAVALIFGL FLTNPAPICV LDEVDAPLDD
ANIERFCDLL EAMTKETDTR YLVVTHNAVT MSRMHRLFGV TMVERGISRL VSVDLVAAEQ
LLAAE
//