ID A0A1M6E429_9RHOB Unreviewed; 1150 AA.
AC A0A1M6E429;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE RecName: Full=Chromosome partition protein Smc {ECO:0000256|HAMAP-Rule:MF_01894};
GN Name=smc {ECO:0000256|HAMAP-Rule:MF_01894};
GN ORFNames=SAMN05444417_1790 {ECO:0000313|EMBL:SHI80252.1};
OS Wenxinia saemankumensis.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Wenxinia.
OX NCBI_TaxID=1447782 {ECO:0000313|EMBL:SHI80252.1, ECO:0000313|Proteomes:UP000184292};
RN [1] {ECO:0000313|EMBL:SHI80252.1, ECO:0000313|Proteomes:UP000184292}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 100565 {ECO:0000313|EMBL:SHI80252.1,
RC ECO:0000313|Proteomes:UP000184292};
RA Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL Submitted (NOV-2016) 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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; FQYO01000003; SHI80252.1; -; Genomic_DNA.
DR RefSeq; WP_073328664.1; NZ_FQYO01000003.1.
DR AlphaFoldDB; A0A1M6E429; -.
DR STRING; 1447782.SAMN05444417_1790; -.
DR OrthoDB; 9808768at2; -.
DR Proteomes; UP000184292; 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:UP000184292}.
FT DOMAIN 4..1135
FT /note="RecF/RecN/SMC N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02463"
FT REGION 396..421
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 803..829
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 866..889
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 177..211
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 293..355
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 464..502
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 639..736
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 949..990
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT BINDING 32..39
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
SQ SEQUENCE 1150 AA; 121752 MW; B4A2E796C418878A CRC64;
MRFTRLRLNG FKSFVDPTDL VIHDGLTGIV GPNGCGKSNL LEALRWVMGE NRPTAMRGGG
MEDVIFAGAA TRPARNYAEV SLHIDNSERL APAAFNDADE LDIVRRITRD AGSAYKVGTK
DVRARDVQML FADASTGSHS PALVRQGQIS ELINARPQNR RRILEEAAGI SGLYARRHEA
ELKLKGAEAN LARVDDVIEQ LAAQLASLAR QARTAARYRE IGERLRRAEG LLLYRRWSDA
EAARVSAFAA LRERAAASVA AERDAAAATE AREGAEAALP PLREEDGVAA AILQRLQVQR
DTAEAEAGRA RGAISALTGR LAQIDKDMER ETALNADAGE TIARLRAEAS ALEAAGQGHP
QALAAAEEGA REAAEVLAAR ESDLSAQTEE VARLAARHQS ARRQVEDGRR TLDKAGREAE
RARAALAEAT AKVGSAGTDL AAAEAAEAQA AATARNADST LAAAEAARAE TQGEEAEARA
ARSEAEGEAT ALRAEVAALA RLVDRDRVEG GSVMDLLSVE SGYETALGAA LADDLRAPLA
GPGAATGWAA LPPYDAAQPL PAGARPLAEV VQVPDVLARR IAQVGLVAAA EGPRLQAALR
PGQRLVSAEG DLWRWDGFRA GAADAPSAAA LRLRQVNRLT AMRRDLDAAE AAADAARAAH
EALAGRLSAL TEADAQARAA RRDADRLVAE ANRRLARAEA DRDLAAGRRE SAALAVTRHE
EEAAEAARAL AAAEAGAEKL GDLEAARGVA ADLKTTVEAA RITMMSRRSA LDETRREGEA
RARRAAEVAR ELATWTGRLD TASKRADELS QRRDQTESQL AEARRRPDEI AARQAETAKA
IAEAESRRAG AAEALEAAEA ALRGAALHER DAERAASDSR EARAGAEARA EAARETVAAA
EARIAEALET TPAALADTLG GTEGLPPADA IEGEVAALRR QRDGLGAVNL RAEEDAREVQ
AEHDTLVTEK ADLEAAIATL RSGIASLNKE GRERLLTAFD EVNGNFSTLF THLFGGGEAK
LTLVESDDPL EAGLEILCQP PGKKLSTLSL LSGGEQTLTA LALIFAVFLA NPAPICVLDE
VDAPLDDANV TRFCDLLDEM TRRTRTRFLI ITHHAVTMSR MDRLFGVTMG EQGVSQLVSV
DLRKAEALVA
//
