ID A0A0K1XG87_9GAMM Unreviewed; 1164 AA.
AC A0A0K1XG87;
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 ORFNames=AKN88_09765 {ECO:0000313|EMBL:AKX60182.1};
OS Thiopseudomonas alkaliphila.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Thiopseudomonas.
OX NCBI_TaxID=1697053 {ECO:0000313|EMBL:AKX60182.1, ECO:0000313|Proteomes:UP000063953};
RN [1] {ECO:0000313|EMBL:AKX60182.1, ECO:0000313|Proteomes:UP000063953}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=E5571 {ECO:0000313|EMBL:AKX60182.1,
RC ECO:0000313|Proteomes:UP000063953};
RX PubMed=26679585;
RA Lauer A.C., Nicholson A.C., Humrighouse B.W., Emery B., Drobish A.,
RA Juieng P., Loparev V., McQuiston J.R.;
RT "Genome Sequences of Oblitimonas alkaliphila gen. nov. sp. nov. (Proposed),
RT a Novel Bacterium of the Pseudomonadaceae Family.";
RL Genome Announc. 3:e01474-15(2015).
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}.
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DR EMBL; CP012365; AKX60182.1; -; Genomic_DNA.
DR RefSeq; WP_053101484.1; NZ_CP012365.1.
DR AlphaFoldDB; A0A0K1XG87; -.
DR STRING; 1697053.AKN87_00250; -.
DR PATRIC; fig|1698449.3.peg.1962; -.
DR Proteomes; UP000063953; Chromosome.
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; 2.
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 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; 1.
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:UP000063953}.
FT DOMAIN 3..1148
FT /note="RecF/RecN/SMC N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02463"
FT COILED 170..218
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 258..425
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 651..825
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 868..902
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 1164 AA; 131223 MW; ED16FDA2041AA891 CRC64;
MRLKCIRLAG FKSFVDPTTA YFPSNMTAVV GPNGCGKSNV IDAVRWVLGE SSAKNLRGES
MTDVIFNGSN TRKPISQASI ELVFDNSVGG LLGEYAAYNE ISVRRLVSRD GQSSYFLNGT
KCRRRDITDI FLGTGLGPRS YAIIEQGMIS RLVEAKPEEL RVFLEEAAGI SKYKERRRET
ENRIRRTEEN LARLTDLRQE LGRQVERLER QAADAKTYTE LKSQERQLKA QLMALHWRAL
DAEVRQRDQA LQLQELELER LISEQRQADA LIEQYRQQHF EQNEAFNRQQ ALFYSVSAEV
AKLEQSINHH HQQQRKLQQQ ALEAEQQQRS LAEELAQDQL TLESLIAELA ELEPEARLQQ
EQVAAFRLEL ETLEAEQLQW QQSWEVFTEQ HAAALHQADF EQNRIQQTEV QLSRYAERLR
RHQDEAQLLN IHQQQQALSE NVAQQTLLAE QQAELALSLE GVQEQLSQQH ARIEQSLQLV
EQHSTAQQRL IGQQASLQAL QEAALGTDNQ QLVQWLQQQQ LQNLASLAEQ LTVEPGWEAI
LEALLGAQLQ SFCSTSLPYA AFASAPPESV SFITPSTASL PAAEDELLAK VKCAYDLSPW
LAGIKTADSF AQAQARLATL QAGESIVTAE GYWLGANFIR FFAADAQQAG VLQRAQQLQA
LELQLQQLTQ ELARAKQALQ QQQALLVDLE QQRQQLLATQ QGLANEQAQQ QAQSSILQAR
VEQLQQRQQQ LQQEMGELEE NISLEQEQLA EARLTLEQAI EQMADHTQHK QKLEHTREQL
TAQLRMLRQQ AQQAQHSQHQ LELQLNTLRA QRQSTEQALA RTAQQVARAG SRHQQLQLEL
AEQGDPVTEL QALLEEQLAE RLLADEGLRE ARQQLEQITA QLRQQEQSRL TFEQRVQQLR
DSVQQAQLAG HEVMVRRDNQ QEQIQDSGFA LAALLELLPA SAVISDWEQE LEQVAQAIER
LGAINLAAIE EFQLQSARKA YLDAQDADLN EALHTLQTVI EKIDQETRQR FRDTFERVNS
GLQRLFPKVF GGGNASLELT GDDLLSTGVA IMAQPPGKKN STIHLLSGGE KALTALSLVF
AIFQLNPAPF CMLDEVDAPL DDANVGRYAN LVKEMSDSVQ FIYITHNKIA MEKADQLLGV
TMHEPGCSRL VAVNVEEAAA LAES
//
