ID A0A0Q5R8M2_9SPHN Unreviewed; 1134 AA.
AC A0A0Q5R8M2;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=Chromosome partition protein Smc {ECO:0000256|HAMAP-Rule:MF_01894};
GN Name=smc {ECO:0000256|HAMAP-Rule:MF_01894};
GN ORFNames=ASG11_15220 {ECO:0000313|EMBL:KQS02132.1};
OS Sphingomonas sp. Leaf357.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingomonas.
OX NCBI_TaxID=1736350 {ECO:0000313|EMBL:KQS02132.1, ECO:0000313|Proteomes:UP000051080};
RN [1] {ECO:0000313|EMBL:KQS02132.1, ECO:0000313|Proteomes:UP000051080}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf357 {ECO:0000313|EMBL:KQS02132.1,
RC ECO:0000313|Proteomes:UP000051080};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQS02132.1, ECO:0000313|Proteomes:UP000051080}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf357 {ECO:0000313|EMBL:KQS02132.1,
RC ECO:0000313|Proteomes:UP000051080};
RA Schulze-Lefert P.;
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:KQS02132.1}.
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DR EMBL; LMPM01000002; KQS02132.1; -; Genomic_DNA.
DR RefSeq; WP_055781971.1; NZ_LMPM01000002.1.
DR AlphaFoldDB; A0A0Q5R8M2; -.
DR STRING; 1736350.ASG11_15220; -.
DR OrthoDB; 9808768at2; -.
DR Proteomes; UP000051080; 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:UniProtKB-KW.
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 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:UP000051080}.
FT DOMAIN 3..1117
FT /note="RecF/RecN/SMC N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02463"
FT COILED 161..209
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 291..353
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 389..416
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 648..682
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 1134 AA; 120337 MW; 1FB1AB35D9E76232 CRC64;
MQIKRLRLSG FKSFVDAADL RIEPGLTGIV GPNGCGKSNL LEALRWTMGE TSARSLRGAG
MEDVIFAGTA TRPAREFAEV SMLIEGDDSE ETEIVRRIER GAGSAYRIDG RDVRAKDVAL
LFADAATGAH SPALVSQGRI SAVIAAKPAE RRAMLEEAAG IAGLHVRRKD AEQKLRATEA
NLARLDEVIA DQDARAAALK RQARQAERYR MLSDQIRTAE ARMIFARWRD AAAASDLAKA
EAAAAETKVA ETAEQQRAAA AYQQQATERL GEARAAALAA RDAASEAGHM LAALRTEQAG
VERRLRDLAD AATRLADDRQ REGALAHDAA EALSRLAEEA KALERRIAEA SGRMPGMEAA
LAEAERAGRD AEVALAQALA AQASEAAEAR VAEAALAAAR MRVERSERDL ARVTAEGRAI
GDAAPLEAER AAAVAARAQA LADGEKARAD LTKADTEERT AIDRRDAAQS ARSAAHAELA
ALNSEAAALA KATQPSGRDR VLDTLQPDPG YEHALAAALG DDLEAGLDPA AERFWAGADP
QPGDPAPPPG TERLADHVAA PAALARRLAQ VLVTDSDDGL PLAVGQRLVT RAGVLRRWDG
YVARSGGAAA AERLVRLNRL RSLEAAKPDA VAAVDAADTA LAQIDRTIAE ARGAAHAARS
ALQQAENRAR DAARNEDRAG AALERIDTQC ADLDARRKRI AGDLSEAQGE VEAAAAIKAA
LPDGSATREQ VTALSAQAET RRNAIATARA ERATLERALA QDRDRLASGS GEAKGWRARA
GEAARRIADM DKREAELTRE TATLAGKPTE IATAIATLEA THQTARAEAD IAQSAERHAE
SVLRETEAVA RMAGEALSEA REARAGALAR AENQELRRVE MGRLSGERFE CPAPVLPEKV
GFAADSVGNP QEESKTHERL SVDRERIGPV NLVAESELAE LEAASSGNAG EREELGLAVN
RLRGSIGTLN REGRQRLLAA FEAVNGHFRR LFTTLFNGGS AHLELIDSDD PLEAGLEIMA
QPPGKKLQSL TLLSGGEQAL TAVALIFGLF LTNPAPICVL DEVDAPLDDA NIERFCGLLD
AMTRETRTRY LIVTHNAVTM SRMHRLFGVT MIEQGVSRLV SVDLGGAETL LAAE
//
