ID A0A0L6D022_9RHOB Unreviewed; 1151 AA.
AC A0A0L6D022;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 24-JAN-2024, entry version 29.
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:KNX43043.1};
GN ORFNames=ROTO_04480 {ECO:0000313|EMBL:KNX43043.1};
OS Roseovarius tolerans.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Roseovarius.
OX NCBI_TaxID=74031 {ECO:0000313|EMBL:KNX43043.1, ECO:0000313|Proteomes:UP000037046};
RN [1] {ECO:0000313|Proteomes:UP000037046}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EL-164 {ECO:0000313|Proteomes:UP000037046};
RA Voget S., Bruns H., Wagner-Doebler I., Schulz S., Daniel R.;
RT "Draft Genome Sequence of Roseovarius tolerans EL-164, a producer of N-
RT Acylated Alanine Methyl Esters (NAMEs).";
RL Submitted (JUL-2015) 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:KNX43043.1}.
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DR EMBL; LGVV01000003; KNX43043.1; -; Genomic_DNA.
DR RefSeq; WP_050661429.1; NZ_LGVV01000003.1.
DR AlphaFoldDB; A0A0L6D022; -.
DR STRING; 74031.SAMN04488077_103213; -.
DR PATRIC; fig|74031.6.peg.458; -.
DR OrthoDB; 9808768at2; -.
DR Proteomes; UP000037046; 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 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; 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:UP000037046}.
FT DOMAIN 4..1136
FT /note="RecF/RecN/SMC N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02463"
FT REGION 770..793
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 845..889
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 170..218
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 293..425
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 454..502
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 629..701
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 936..991
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COMPBIAS 864..889
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; 125452 MW; 4D30297B39341CD7 CRC64;
MQFSKLRLTG FKSFVDPTDL IIADGLTGVV GPNGCGKSNL LEALRWVMGE NRPSAMRGGG
MEDVIFAGAA TRPARNFAEV VIHLDNSDRL APAGFNDADH LEIVRRITRD VGSAYKVNTK
DVRARDVQML FADASTGAHS PALVRQGQIS ELINAKPKSR RRILEEAAGI SGLYQRRHEA
ELKLRAAETN LTRVDDVVEQ LAAQLAQLAR QAKQAARYRQ IGEELRLAEG LLLYRRWKEA
DQARARAEED LRERTTAAAR AEAAAREAAK ARTKADDALP ALREEEAIAG AILQRLTVQR
DTLSEQEANA RDRIETLEGR IAQLARDIER ETGLNHDAGE TIKRLDWEAA ELAKGAEGHE
GRLEAAQEEA RDAARVLQER ESDLSQMTED MARLSARHQS AQRLIEDCRK TLAKSETEAE
RARATQAGSL EALRKAETDQ AAAAKAEAEA VAAAEAAEAA LVTADEARAE AQTREAEARA
ARSEAEGEVN ALRAEVTALA KLVERDTAEG GQIMDRLQVQ QGFEKALGAA LADDLRAPEV
GADGPSGWTI LPGYQTPQPL PEGVTALTNH VSVPEVLARR MSQIGLVDAE DAPRLQPLLK
PGQRLVSTEG DLWRWDGFRA WAEDAPSAAA LRLQQLNRLE ELKQQLEHAT ARADGAMRAH
EALREQLAHC TEKDRAAREA RRSADAAVNE ANRALSRAEA DSNLAGSRLE SSGLAVTRHE
EEAMAARKGL AEAENGLSGL GDLEATRADL EDIKMTVEAA RMTMMAKRSA ADELRREGER
RTRRSQEIAK EVSGWRHRLE TAEKRSAELA ERKDASEAEL ADASATPEIL AAKRAELGEE
ITRSEARRAE AADALSTAEG AARQAGLDER EAERQASEAR EARARAEARV DAARETRDLA
AERIGEAMDT TPDALLESLG ADPDTMPGSD AIEADVNRLK RQRDALGAVN LRAEEDAKEV
QEEHDTLVTE KADLEEAIKT LRGGIASLNR EGRERLLTAF EQVNSNFTLL FRHLFGGGEA
NLVLVESDDP LEAGLEIMCQ PPGKKLSTLS LLSGGEQTLT ALALIFAVFL ANPAPICVLD
EVDAPLDDAN VTRFCDLLDE MCRRTETRFL IITHHAVTMS RMDRLFGVTM AEQGVSQLVS
VDLKKAEAMV A
//
