ID A0A2K1PZI1_9GAMM Unreviewed; 1167 AA.
AC A0A2K1PZI1;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE RecName: Full=Chromosome partition protein Smc {ECO:0000256|HAMAP-Rule:MF_01894};
GN Name=smc {ECO:0000256|HAMAP-Rule:MF_01894};
GN ORFNames=Lysil_2382 {ECO:0000313|EMBL:PNS08206.1};
OS Lysobacter silvestris.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Lysobacter.
OX NCBI_TaxID=1645665 {ECO:0000313|EMBL:PNS08206.1, ECO:0000313|Proteomes:UP000236220};
RN [1] {ECO:0000313|EMBL:PNS08206.1, ECO:0000313|Proteomes:UP000236220}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AM20-91 {ECO:0000313|EMBL:PNS08206.1,
RC ECO:0000313|Proteomes:UP000236220};
RA Zhang D.-C., Albuquerque L., Franca L., Froufe H.J.C., Barroso C., Egas C.,
RA Da Costa M., Margesin R.;
RT "Lysobacter sylvestris genome.";
RL Submitted (AUG-2017) 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. SMC3 subfamily.
CC {ECO:0000256|ARBA:ARBA00005917}.
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:PNS08206.1}.
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DR EMBL; NPZB01000002; PNS08206.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2K1PZI1; -.
DR OrthoDB; 9808768at2; -.
DR Proteomes; UP000236220; 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; 1.10.287.1490; -; 1.
DR Gene3D; 1.20.1060.20; -; 1.
DR Gene3D; 3.30.70.1620; -; 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; IPR010935; SMC_hinge.
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; PF06470; SMC_hinge; 1.
DR Pfam; PF02463; SMC_N; 1.
DR PIRSF; PIRSF005719; SMC; 1.
DR SMART; SM00968; SMC_hinge; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF75553; Smc hinge domain; 1.
DR SUPFAM; SSF57997; Tropomyosin; 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:UP000236220}.
FT DOMAIN 521..619
FT /note="SMC hinge"
FT /evidence="ECO:0000259|SMART:SM00968"
FT COILED 170..211
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 244..330
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 466..500
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 660..792
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 1167 AA; 128552 MW; B1030BE568A69273 CRC64;
MRLSTIKLAG FKSFVDPTTL HLPTNMTGIV GPNGCGKSNI IDAVRWVMGE SSASRLRGDN
ATDVIFSGSN ARKPVSQATV ELIFDNGDHA ITGEYAAFNE ISVKRSVGRD GQSQYYLNGT
KCRRRDITDL FLGTGLGPRS YSIIEQGMIS QIIEAKPEEL RVYLEEAAGI SKYKERRRET
ETRIRHTREN LERLTDLRDE VGKQLQHLAR QAKQAEQYTA LQSERLVKDA EWKALQFRAL
DVQLQTHRQA LAADETRLEQ LVAEQREAER QIETGRIRHQ EATDVHAKAQ AEVYEVGGTL
ARIEQQIHHQ KEMSSRLQQA RSEAEAALME LVGHISGDGD KLAALKAALE ESEPRLAQLK
ADDETKQAAL RDADAALADL QQRWDTHVRE QNEAARSGDV DRTRVDYLDR QLLDGERRRE
KLEAERSGHD LDALANAFAE AQQGHDTHKA ALDGLTSDLE TRKATVTQLQ EDQRTAQGEL
AEVRKELQGA RGRLSSLEAL QHAALGQEQG AAVEWLKKHG LDSARRVGET LDVQEGWEAA
VEGALGQMIE GVLVESPEAL VEALGELGEG RLTLVSPDAG NDEFADTSLA ARVKGPLAIR
RLLANLHVAE TLPEARALLA TLGEGASVIT RAGERLGPGW VRVMRSGAVK QGALIRGREI
QSLRSSIDAL QGRERELDQK IASSRDRALA AEQEREDAQR ALYHAHRNVS ELAGRLQSQQ
GRLQSARDRI AAIETELAQI AQAGGEAQAG AREARARLES TVERMAGLEQ ARAALEAERR
SFSEQRDAAR HAARESRDAL HALQLSLESQ RAQVVSLMQS LDRMGSQRGQ LDTRLGELVG
QLAEGDSPVQ ALDQQRQAAL AERVRVDQGL TAARAKLEAI DNELREFEQT RQQRDSHSIT
QREAISQRKL DQQALALAAE QLRVAVTGAG FALDDVINTL DENADAQAWE RVVGDLETRM
RRLEPVNLAA IQEHAESAQR KEYLDAQDAD LTTALDTLED AIRKIDRETR GRFKDTFDRV
NAGVQELYPR LFGGGHAYLE LTGEDLLDTG VAIMARPPGK RVSNISLLSG GEKAMTAVAL
VFAIFRLNPA PFCLLDEVDA PLDEANVGRF TTMVKEMSDA VQFLFVTHNK ATMEAAEQML
GVTMREAGVS RMVSVDLAEA SRLAGVA
//
