ID A0A0F3GPW3_9BACT Unreviewed; 1159 AA.
AC A0A0F3GPW3;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE RecName: Full=Chromosome partition protein Smc {ECO:0000256|HAMAP-Rule:MF_01894};
GN Name=smc {ECO:0000256|HAMAP-Rule:MF_01894};
GN ORFNames=MBAV_005078 {ECO:0000313|EMBL:KJU82728.1};
OS Candidatus Magnetobacterium bavaricum.
OC Bacteria; Nitrospirota; Nitrospiria; Nitrospirales; Nitrospiraceae;
OC Magnetobacterium.
OX NCBI_TaxID=29290 {ECO:0000313|EMBL:KJU82728.1, ECO:0000313|Proteomes:UP000033423};
RN [1] {ECO:0000313|EMBL:KJU82728.1, ECO:0000313|Proteomes:UP000033423}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TM-1 {ECO:0000313|EMBL:KJU82728.1};
RA Kolinko S., Richter M., Glockner F.O., Brachmann A., Schuler D.;
RT "Single-cell genomics of uncultivated deep-branching MTB reveals a
RT conserved set of magnetosome genes.";
RL Submitted (FEB-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. 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:KJU82728.1}.
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DR EMBL; LACI01002192; KJU82728.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0F3GPW3; -.
DR PATRIC; fig|29290.4.peg.6687; -.
DR Proteomes; UP000033423; 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 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.
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:UP000033423}.
FT DOMAIN 534..656
FT /note="SMC hinge"
FT /evidence="ECO:0000259|SMART:SM00968"
FT REGION 88..114
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 297..324
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 360..436
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 721..776
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 833..860
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 917..944
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 997..1038
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COMPBIAS 88..110
FT /note="Polar 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 1159 AA; 129157 MW; 40015DA367A2A768 CRC64;
MKIVKLQLNG FKSFAEKTSF TMHSGVTCIV GPNGSGKSNV VDAFRWVLGE QSAKTLRGDK
MEEVIFNGTS DTAPKGMAEV TLSLSDIKGN ETADNSSDKV SDNGTGKAHG DSSSGADIVE
VTRRLYRSGE SEYYINKAKA RLKDVRELFL DTGLEVKSYS ILEQGRISEI LNAKPVERRS
LIEEVAGVMK YKVRKSEAIT KLQRASLNLE RVNDIVSEVK RSVGSLERQA KKAERYKSLG
AQLSSIELRI ARRDYDALSS ACKALDLLHA DYTGRLGELT AEVAHNEELK TKHGAGLKDK
KQVLDKTLHA ISEMERQLSG TEKDMAVKDS TLNNILSHIQ RLSAQQTEYL QQQYETIDRM
EELSEVESEL HREIEVIEAE YQSDKDKIEG IEKAFASIET EVRDKNRDFY QLSEQISNVR
NEVSTLQTHL GALQQRQESS GSFFRGAQQT LDKHDSDIEA TRKDIVDSQE GLALATERRQ
LLTTQLKQSD LSIERLRQGI AARRESIASD KARLKSLQEI TASTLHEKDF GGTINIVATL
SATLEVPQQY EIAVESALSD KVLAVILGTE GELKGAVAFI KQRAWDRTAL ISLDLYPSSD
PSHKGMETEE KEQGLADGDV RALDVIKVDD AYRTVVGQLL GGVVIVCDID RALELFRGNG
GGHYVTLDGD VLGRDGVLTA GKGTDVLRHL RNIRELTEGL DISAEALAGL ERDLASAISE
RDWLRTEQQE VQEQLASLDK EVSIFNLNLK KLTEERDRLA KKMHYMEVEA RQTEQEVQSV
LAAIKEKGQH QDILSARKDE TAVYLQGLRD SLSSHKALIE TTRTSLTDKK VALTTKKERL
KSVQKEASSL RRAAEAIADK LSAIAQESGT LTSRRQEIAN DIEVGAVDLQ RISQDVALLR
QQAAQEKGVI DVEGNTLAEI DRTLTKLRHD NDLLKEQLNE TDVQRMQHNL RMENIRTSVS
NTYDKDILEV EPQPLQEGEE DIVGELRRKI AEMGAVNMAS IEEYEELKRR YDFLLAQQED
LLKSIAELEQ AIAKINSTTR KMLTESFYEL NIKFNETFQE FFGGGKAELT LTDPSNILES
GIEIAVQPPG KKLQNINLLS GGEKSLSALS LIFAGFLIKP TPMCILDEAD AALDESNTRR
FSDTLKTPLS FFFSSTAWR
//
