ID A0A0P7XL98_9RHOB Unreviewed; 1151 AA.
AC A0A0P7XL98;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 31.
DE RecName: Full=Chromosome partition protein Smc {ECO:0000256|HAMAP-Rule:MF_01894};
GN Name=smc {ECO:0000256|HAMAP-Rule:MF_01894,
GN ECO:0000313|EMBL:KPQ17456.1};
GN ORFNames=HLUCCO18_04370 {ECO:0000313|EMBL:KPQ17456.1};
OS Rhodobacteraceae bacterium HLUCCO18.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae.
OX NCBI_TaxID=1666917 {ECO:0000313|EMBL:KPQ17456.1, ECO:0000313|Proteomes:UP000050333};
RN [1] {ECO:0000313|EMBL:KPQ17456.1, ECO:0000313|Proteomes:UP000050333}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HLUCCO18 {ECO:0000313|EMBL:KPQ17456.1};
RA Nelson W.C., Romine M.F., Lindemann S.R.;
RT "Identification and resolution of microdiversity through metagenomic
RT sequencing of parallel consortia.";
RL Submitted (SEP-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:KPQ17456.1}.
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DR EMBL; LJSY01000007; KPQ17456.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0P7XL98; -.
DR STRING; 1666917.HLUCCO18_04370; -.
DR PATRIC; fig|1666917.4.peg.651; -.
DR Proteomes; UP000050333; 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 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; 2.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 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|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}.
FT DOMAIN 4..1136
FT /note="RecF/RecN/SMC N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02463"
FT REGION 406..430
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 464..492
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 170..204
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 251..362
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 632..753
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 799..826
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 865..903
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 950..991
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COMPBIAS 464..484
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 32..39
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
SQ SEQUENCE 1151 AA; 124665 MW; FBF01EA6D287B83C CRC64;
MRFNKLRLNG FKSFVDPTDL VIGDGLTGVV GPNGCGKSNL LEALRWVMGE NRPTAMRGDG
MEDVIFAGAA TRPARNFAEV HVQIDNAQRL APAGFNDADQ IDIVRRITRD AGSAYKLNGK
DVRARDVQML FADAATGAHS PALVRQGQIA ELINAKPKNR RRVLEDAAGI AGLYQRRHEA
ELKLRGAEQN LARIDDVLEQ LAGQIATLAR QAKQAARYRE IGADLRAAEG LLLWLRWRDA
DATRLSAEEV LRAALSDAAR AEKAARDASE AREAAETALP PLREEDTIAA AVLQRLYVER
DSIDAEARRA AEEVASLEAR IAQLARDLDR ETALNADAGD TIARLEAEAL TLREAMEGHA
EALEAASAEA VAANDILGER EGALARETEL QADLAARHQA ADRRIAEARQ ARARHEAEAE
KATRAAREGV DRLASLSRDV EAAGQALQEA TDLAARAEAT LAETEAARAE AEGREAETRA
ARSEAEGRAA TLSSEVASLT RLLDRDRGPQ KAIVDDMSVT GGFETALGAA LADDLNAPQS
GKAGESGWSV LPDYDETAPL PAEAEPLAFH VDAPAALSRR LSQIGLVSAA DGPRLQALLR
PGQRLVSREG DLWRWDGYTV AAADAMSGAA RRLEQKNRLA VLTDEAAEAE AQASAAREAH
ETWAKRLSDL NGADRQARDA RRQAETNLAA ASRAQTRAET ERATLDARLD TLRETARRHA
EQVEAAIADV AEAEETKAAL EDLEIVRARL GDRRMTVDAA RITMMARRGE HDELRREGER
REKRLTQIAD ELGTWRNRLA SAETQLGDLS RRKSEAEDAL EVARTRPAEI EARRSTLGQG
ITDAEARRAK AADALAGGER ANTEAVAAER AAERAASEAR EARAAAEARR DAAAEAVEAA
AARISEELET TPEDLREKLG DLPDPLPRAD RIEADVHRLR RQRDALGAVN LRAEEDAKTV
QEEHDTLLHE KEDLEAAIAK LRSGIASLNR EGRSRLLTAF EQVNVNFAKL FTHLFGGGEA
RLVLVESDDP LEAGLEILCQ PPGKKLSTLS LLSGGEQTLT ALALIFAVFL ANPAPICVLD
EVDAPLDDAN VGRFCDLLDE MTRQTETRFL IITHHAVTMA RMDRLFGVTM AEQGVSQLVS
VDLKKAEAMV A
//
