ID A0A0Q4G6T4_9SPHN Unreviewed; 1132 AA.
AC A0A0Q4G6T4;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE RecName: Full=Chromosome partition protein Smc {ECO:0000256|HAMAP-Rule:MF_01894};
GN Name=smc {ECO:0000256|HAMAP-Rule:MF_01894};
GN ORFNames=ASE72_04960 {ECO:0000313|EMBL:KQM73919.1};
OS Sphingomonas sp. Leaf20.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingomonas.
OX NCBI_TaxID=1735685 {ECO:0000313|EMBL:KQM73919.1, ECO:0000313|Proteomes:UP000051642};
RN [1] {ECO:0000313|Proteomes:UP000051642}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf20 {ECO:0000313|Proteomes:UP000051642};
RA Garrido-Oter R., Mueller D.B.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000051642}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf20 {ECO:0000313|Proteomes:UP000051642};
RA Vorholt J.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-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:KQM73919.1}.
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DR EMBL; LMKN01000001; KQM73919.1; -; Genomic_DNA.
DR RefSeq; WP_056017391.1; NZ_LMKN01000001.1.
DR AlphaFoldDB; A0A0Q4G6T4; -.
DR STRING; 1735685.ASE72_04960; -.
DR OrthoDB; 9808768at2; -.
DR Proteomes; UP000051642; 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:UP000051642}.
FT DOMAIN 3..1115
FT /note="RecF/RecN/SMC N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02463"
FT REGION 529..552
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 164..205
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 646..673
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 1132 AA; 119102 MW; 133F9813E8205A6A CRC64;
MQIKRLRITG FKSFVEPADL RIEPGLTGVV GPNGCGKSNL LEALRWTMGE ASAKSLRGSG
MEDVIFAGTA TRPPRDFAEV SILAEIAGPT GVDECEVVRR IERGAGSAYR IDGRDVRAKD
VGLLFADAAT GAHSPALVSQ GRIGAVIAAK PADRRAMLED AAGIAGLHVR RKDAEARLRA
TEANLARLDE VIADQDARVA ALRRQARAAD RYRQLSTQIR VAEARLVFAR WQEAATAADA
ARLAAAVADA RVSDAAAIER TTAANRLDAA AAVATARSAA LAARDTATET GHALASLRTE
RAAIDRQLTG LADARRRIAE DRAREGSLAR DAADALARLA DETTALDAAI TQATAAVPAL
DAAQVEAERR ARDAEVALAQ AMTRHAGDVA ETRVAAAALA AAGARADRAA RDAAQLGAAR
AALGDAAPIE AERDAAAAAR LAAIEEAAAA RHALGQAETD ERDAIAARDA AESARATARA
DLTAIDSEAA ALTRATQRSG RDRLLDHVTA TPGHERALAA ALGDDLDTPH AAWTGATPRA
DDPTAPPGAT PLAAQVDAPA VLARRLAQVF VTEVDEGSPL AVGQRLVTRD GTLRRWDGFV
ATGSGAAAAE RLERLNRLHA LQAARPAAAD AVATRDAERS AIDQDIAAAR RAAQDARTRL
AAAETRVRDA QRTEDRAAAL LERLVGQRAD LDLRAHRIDT EQDAARAEQR AADAAVAALP
DARASADAVA GLHRTAEACR TAVAQARGAR GALDRSRATD RERLAAAHAD IRSWRARAGE
AAKRIGAMDL REVDLARDAD RIADRPAALD RQLAALDADT AAARATADTL HAAEQAADAA
LRAAEDGQRL AAETLATARE NRAAAATRAD NHEQRRIEAG RVSGQRFECP APLLPERLGF
AAADVRSPED ETRGFERLTT DRERIGAVNL MADRELAELE SASGGNAAER AELGEAVQRL
RGSIGTLNRE GRQRLLTAFA AVNDHFQRLF GTLFDGGAAH LDLVDSDDPL EAGLEILAQP
PGKRLQSLTL LSGGEQALTA VALIFALFLT NPAPICVLDE VDAPLDDANI DRFCALLDRM
ARDTATRYLV VTHNAVTMSR MHRLFGVTMI EPGVSRLVSV DLQAATDLVA VA
//
