ID Q79GE1_BORPE Unreviewed; 1175 AA.
AC Q79GE1;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 27-MAR-2024, entry version 60.
DE RecName: Full=Chromosome partition protein Smc {ECO:0000256|HAMAP-Rule:MF_01894};
GN Name=smc {ECO:0000256|HAMAP-Rule:MF_01894};
GN OrderedLocusNames=BP3558 {ECO:0000313|EMBL:CAE43817.1};
OS Bordetella pertussis (strain Tohama I / ATCC BAA-589 / NCTC 13251).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae; Bordetella.
OX NCBI_TaxID=257313 {ECO:0000313|EMBL:CAE43817.1, ECO:0000313|Proteomes:UP000002676};
RN [1] {ECO:0000313|Proteomes:UP000002676}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tohama I / ATCC BAA-589 / NCTC 13251
RC {ECO:0000313|Proteomes:UP000002676};
RX PubMed=12910271; DOI=10.1038/ng1227;
RA Parkhill J., Sebaihia M., Preston A., Murphy L.D., Thomson N.R.,
RA Harris D.E., Holden M.T.G., Churcher C.M., Bentley S.D., Mungall K.L.,
RA Cerdeno-Tarraga A.-M., Temple L., James K.D., Harris B., Quail M.A.,
RA Achtman M., Atkin R., Baker S., Basham D., Bason N., Cherevach I.,
RA Chillingworth T., Collins M., Cronin A., Davis P., Doggett J., Feltwell T.,
RA Goble A., Hamlin N., Hauser H., Holroyd S., Jagels K., Leather S.,
RA Moule S., Norberczak H., O'Neil S., Ormond D., Price C., Rabbinowitsch E.,
RA Rutter S., Sanders M., Saunders D., Seeger K., Sharp S., Simmonds M.,
RA Skelton J., Squares R., Squares S., Stevens K., Unwin L., Whitehead S.,
RA Barrell B.G., Maskell D.J.;
RT "Comparative analysis of the genome sequences of Bordetella pertussis,
RT Bordetella parapertussis and Bordetella bronchiseptica.";
RL Nat. Genet. 35:32-40(2003).
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}.
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DR EMBL; BX640421; CAE43817.1; -; Genomic_DNA.
DR RefSeq; NP_882071.1; NC_002929.2.
DR RefSeq; WP_010931537.1; NZ_CP039022.1.
DR AlphaFoldDB; Q79GE1; -.
DR STRING; 257313.BP3558; -.
DR PaxDb; 257313-BP3558; -.
DR GeneID; 69600444; -.
DR KEGG; bpe:BP3558; -.
DR PATRIC; fig|257313.5.peg.3851; -.
DR eggNOG; COG1196; Bacteria.
DR HOGENOM; CLU_001042_2_2_4; -.
DR Proteomes; UP000002676; Chromosome.
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; 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:UP000002676}.
FT DOMAIN 518..625
FT /note="SMC hinge"
FT /evidence="ECO:0000259|SMART:SM00968"
FT COILED 170..218
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 244..341
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 405..506
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 659..686
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 722..894
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 992..1023
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 1175 AA; 130675 MW; DDAE60E2682EA5DA CRC64;
MRLTQLKLAG FKSFVDPTVI PVPSQLVGVV GPNGCGKSNI IDAVRWVLGE AKASELRGES
MQDVIFNGSG NRKPAARASV EMVFDNTEGR AAGQWSAYSE IAVRRVLTRD GTSSYYVNNQ
QVRRRDIHDI FLGTGLGARG YAIIGQGMIN RLIEARPEEL RVFLEEAAGV SRYKERRRET
ENRLSDTREN LTRVEDILRE LGSQLDKLEA QAEVARKYRE LQADGEKKQF ALWLLKETGA
RDERERKNQD MARAQNDLEA AIAGLRAGEA ELESRRQAHY AASDAVHAAQ GQLYEANAQV
SRLEAEIRHV VDSRNRLQAR REQLQAQIAE WNTQQEHCTE QIALAEEDLA TGAARTEEAR
AAAEDAQAGL PAIEARVRDA AAGRDDMRAA LARVEQNLAL VAQTQRDADR QLQTLEQRRE
RLQQELRELH TPDPERLEQL AGDRLAGEDQ LEAAQAELAT LEGRVPEADA ERSRAQAAAQ
QDAQGLARLE ARLAALVKLQ EDVQKQGALE PWLAKHELAG LGRLWQKLHI EPGWETALEA
ALRERMAALE VRSLDWARAF ADDAPPARLA FYQVPVAAPA PAAPQGQTPL ASLLRVTDPD
LRTLLNQWLA GLYTAADLTQ ALGGRASLPA GAAYVVKAGH LVDAHSVRFY APDSEQAGLL
ARQQEIENLQ REIKAQQLIA DQARAAVARA EAAWQQVSQA IAPARQRVVE VTRRVHDIQL
EHSRLQQQAE QSGERAARLR QDLEELAAHE EDLRATREEA EVRFEALDGE LAEHQSRFSD
AEIDGETLSA QADAARTRLR ELERAAQEAE FAERGVQVRI TDLQRNRQLA ADQSQRAATE
LQQLETDLVD LDASASQAGL QDALELRAER EEALTRARLE LDNLSALMRG ADEERMQQER
GLEPLRARIT ELQLQEQAAR LAEEQFTEQL NAREVDRETL ARELAEMPDE WRKASWLQSE
VGRISRQVDA LGPVNLAALD ELNTSRERKT FLDAQQQDLL TAMETLEDAI RKIDRETREL
LQETFNTVNR HFGELFPKLF GGGEARLTMT GDEILDAGVQ VMAQPPGKRN STIHLLSGGE
KALTATALVF ALFKLNPAPF CLLDEVDAPL DDANTERYAN LVSNMSEQTQ FLFISHNKIA
MQMAKQLIGV TMQEQGVSRI VAVDIDSAVQ MAAEA
//
