SMC_BORPD
ID SMC_BORPD Reviewed; 1176 AA.
AC A9II65;
DT 31-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT 31-MAY-2011, sequence version 2.
DT 03-AUG-2022, entry version 72.
DE RecName: Full=Chromosome partition protein Smc {ECO:0000255|HAMAP-Rule:MF_01894};
GN Name=smc {ECO:0000255|HAMAP-Rule:MF_01894}; OrderedLocusNames=Bpet1704;
OS Bordetella petrii (strain ATCC BAA-461 / DSM 12804 / CCUG 43448).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae; Bordetella.
OX NCBI_TaxID=340100;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-461 / DSM 12804 / CCUG 43448;
RX PubMed=18826580; DOI=10.1186/1471-2164-9-449;
RA Gross R., Guzman C.A., Sebaihia M., Martin dos Santos V.A.P., Pieper D.H.,
RA Koebnik R., Lechner M., Bartels D., Buhrmester J., Choudhuri J.V.,
RA Ebensen T., Gaigalat L., Herrmann S., Khachane A.N., Larisch C., Link S.,
RA Linke B., Meyer F., Mormann S., Nakunst D., Rueckert C.,
RA Schneiker-Bekel S., Schulze K., Voerholter F.-J., Yevsa T., Engle J.T.,
RA Goldman W.E., Puehler A., Goebel U.B., Goesmann A., Bloecker H., Kaiser O.,
RA Martinez-Arias R.;
RT "The missing link: Bordetella petrii is endowed with both the metabolic
RT versatility of environmental bacteria and virulence traits of pathogenic
RT Bordetellae.";
RL BMC Genomics 9:449-449(2008).
CC -!- FUNCTION: Required for chromosome condensation and partitioning.
CC {ECO:0000255|HAMAP-Rule:MF_01894}.
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01894}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|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 SMC hinge
CC near the middle of the molecule. These domains are separated by coiled-
CC coil structures. {ECO:0000255|HAMAP-Rule:MF_01894}.
CC -!- SIMILARITY: Belongs to the SMC family. {ECO:0000255|HAMAP-
CC Rule:MF_01894}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAP42043.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AM902716; CAP42043.1; ALT_INIT; Genomic_DNA.
DR AlphaFoldDB; A9II65; -.
DR SMR; A9II65; -.
DR STRING; 94624.Bpet1704; -.
DR EnsemblBacteria; CAP42043; CAP42043; Bpet1704.
DR KEGG; bpt:Bpet1704; -.
DR eggNOG; COG1196; Bacteria.
DR Proteomes; UP000001225; 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:0006260; P:DNA replication; IEA:UniProtKB-UniRule.
DR GO; GO:0007062; P:sister chromatid cohesion; IEA:InterPro.
DR Gene3D; 3.40.50.300; -; 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 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; SSF52540; 1.
DR SUPFAM; SSF75553; SSF75553; 1.
DR TIGRFAMs; TIGR02168; SMC_prok_B; 1.
PE 3: Inferred from homology;
KW ATP-binding; Coiled coil; Cytoplasm; DNA-binding; Nucleotide-binding;
KW Reference proteome.
FT CHAIN 1..1176
FT /note="Chromosome partition protein Smc"
FT /id="PRO_0000409264"
FT DOMAIN 521..623
FT /note="SMC hinge"
FT COILED 169..506
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01894"
FT COILED 653..947
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01894"
FT COILED 987..1024
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01894"
FT BINDING 32..39
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01894"
SQ SEQUENCE 1176 AA; 130561 MW; A5656D9CBD9CFCFB CRC64;
MRLTQLKLAG FKSFVDPTVI PVPSQLVGVV GPNGCGKSNI IDAVRWVLGE AKASELRGES
MQDVIFNGSG NRKPAARASV EMVFDNSEGR AAGQWSTYSE IAVRRVLTRD GTSSYYVNNQ
QVRRRDIHDI FLGTGLGARG YAIIGQGMIN RLIEARPEEL RVFLEEAAGV SRYKERRRET
ENRLSDTREN LTRVEDILRE LGSQLEKLEA QAEVARQYRE LQADGEKKQF ALWLLKETGA
RDERQRKSQE MAQAQTNLEA AIANLRSGEA ELESRRQAHY AAGDAVHAAQ GQLYEANAQV
SRLEAEIRHV VDSRNRLQAR REQLQQQIAE WDAQQTHCVE QIAQAEDDLA TGAARTEEAR
ALAEEAHASL PAVEARVRDA AASRDEMRSS LARVEQNLAL AAQTQRDADR QLQNLEQRRE
RLQQELRELH APDPVRLEQL AGDRAAGEDQ LEEAQQELAA LEARVPEADA ERSRAQAAAQ
QDAQNLARLE ARLAALVKLQ EDVQKQGALE PWLAKHELAG LGRLWQKLHI EPGWENALEA
VLRERMAALE VRNLDWSRAF AEDAPPARLA FYQMPAAAPT PAAPQGLTPL ASLLRITDPD
LRTLLNDWLG NIYTAPDLGQ ALAARATLPA GAACVVPAGH LVDAHSVRFY APDSEQAGLL
ARQQEIENLQ REIKAQQLIA DQARAAVARA ESAWQQVSQA VAPARQRVAE ITRRVHDIQL
EHSRLQQQAE QSGERAARLR QDLEEISAHE EDLRATREEA EARFEALDAE LAEHQSRFAD
AEIAGEDLAA QAEAARARLR ELERAAQEAE FAERGVQSRI ADLQRNRQLA ADQSQRAAVE
LEQLQADLAD LDASASQAGL QDALEVRAER EEALSRARQE LDNLSALLRG ADEERMQQER
ALEPLRARIT ELQLQEQAAR LAEEQFTEQL NAREVDREAL AQELAAMPDE WRRANWLQSE
VGRISRQIDS LGSVNLAALD ELNASRERKE FLDSQQQDLL TAIDTLEDAI RKIDRETREL
LQATFDTVNG HFGELFPKLF GGGEAKLTMT GDEILDAGVQ VMAQPPGKRN STIHLLSGGE
KALTATALVF ALFKLNPAPF CLLDEVDAPL DDANTERYAN LVSSMSEQTQ FLFISHNKIA
MQMAKQLVGV TMQEQGVSRI VAVDIDSAVQ MAAEAA