ID A0A0W1A9B3_9GAMM Unreviewed; 1164 AA.
AC A0A0W1A9B3;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE RecName: Full=Chromosome partition protein Smc {ECO:0000256|HAMAP-Rule:MF_01894};
GN Name=smc_1 {ECO:0000313|EMBL:KTD77934.1};
GN Synonyms=smc {ECO:0000256|HAMAP-Rule:MF_01894};
GN ORFNames=Lwor_1816 {ECO:0000313|EMBL:KTD77934.1};
OS Legionella worsleiensis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Legionellales;
OC Legionellaceae; Legionella.
OX NCBI_TaxID=45076 {ECO:0000313|EMBL:KTD77934.1, ECO:0000313|Proteomes:UP000054662};
RN [1] {ECO:0000313|EMBL:KTD77934.1, ECO:0000313|Proteomes:UP000054662}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49508 {ECO:0000313|EMBL:KTD77934.1,
RC ECO:0000313|Proteomes:UP000054662};
RA Burstein D., Amaro F., Zusman T., Lifshitz Z., Cohen O., Gilbert J.A.,
RA Pupko T., Shuman H.A., Segal G.;
RT "Genomic analysis of 38 Legionella species identifies large and diverse
RT effector repertoires.";
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:KTD77934.1}.
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DR EMBL; LNZC01000022; KTD77934.1; -; Genomic_DNA.
DR RefSeq; WP_058493599.1; NZ_UGPA01000001.1.
DR AlphaFoldDB; A0A0W1A9B3; -.
DR STRING; 45076.Lwor_1816; -.
DR PATRIC; fig|45076.6.peg.1976; -.
DR OrthoDB; 9808768at2; -.
DR Proteomes; UP000054662; 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; 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; 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; 2.
DR PIRSF; PIRSF005719; SMC; 1.
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:UP000054662}.
FT DOMAIN 3..131
FT /note="RecF/RecN/SMC N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02463"
FT DOMAIN 374..1150
FT /note="RecF/RecN/SMC N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02463"
FT COILED 170..225
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 300..493
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 660..687
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 744..778
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 807..841
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; 133243 MW; 2CDDD5EABE6753B0 CRC64;
MQLKQLKLAG FKSFVDPTVV HFPSQLVAVV GPNGCGKSNI IDAVRWVMGE SSAKNLRGDS
MTDVIFNGSS QRKSVGQASV ELVFDNSLGR LSGPFASYGE IAVKRIVTRD GESSYFLNGS
RCRKKDITDI FLGTGAGVKG YSIIGQGTIS RLIEAKPEEL RAFLEEAAGV SKYKERRRET
LQRIEHTRDN LTRVADIREE LDKQLQRLER QAKSAERYTV LKEEERLCKA EILALRWQEF
TQQQQIKQRE LQQLAVRYEE QQSLLTASGK ERTVLNEQLQ DATEQSQYIQ ETFYQTGTEI
ARLEETIQQK ERDKKRLEHD RQQMQQDWQS AASQLKRDKE ELVNAQQRAQ NLAGDLDALK
RDFTARECAQ EEAQQQQKEW EQRWQEVQIN TNTVRSELNV TQINRQHLEQ RRQQTQLRLE
KLESEKNAIS LEQLEQTKRD LEHQRTQLSE TQLFDEEQLR LGNEHINQHR LQLQETEQQL
HQLQDDFHRL NSEHAALIAI QKAARQANKT SKEGIKTWGE KSRLMDVLQV APQWQSVCEM
VLGDDLHAYV LDDFDELWPQ WSECVRLGES VVTLNDVSCN KSSHPRLSDQ ISGSIPATFK
NVHHIYTAEH LDEARSWLPE LSDHESVVTV DGFWLGKGWV KLVNRGAHDE MGLLARQQRI
TELNLIVAEL QQQIESVRSL RDQHHAQLQQ SIKRLEAYQL NLNASNDALR ANSSALAGNE
HAMQHAQRIM GTIAAESEDL AFLIEELATE QLKLDERLHD LEQQYQEAEQ QQFNAAAEKQ
AFADAVTAQN KLVAELRSMV HQTELEYDRE TIKIQQVTDR ISREQERLNV LEERLEHLAM
LCMQSAEPDA ELQEHLAELL LKHGEVESQL SLSRERLAQF RIELEKLDKA TIAYDLEMKR
IQDVIGQTRM EEHALSVRAS SVQESLDELD LKADILLELI PPGTTQTMRE EELIAITERI
KRLGAINLAA IEEYAAEQQR KIYLDEQHED LSQALATLET AIEKMDKETR LRLENTFDEV
NTSFKALFPR LFGGGRAQLE LTCDNLLEAG IVVMAQPPGK RNSTIHLLSG GEKAMTAVAL
VFAIFQLNPS PFCMLDEVDA PLDDVNVGRF CDLVREMSQF VQFLFITHNK VTMELADHLI
GVTMREPGVS RLVAVDVKHA LTME
//