ID F7T3J6_9BURK Unreviewed; 1159 AA.
AC F7T3J6;
DT 21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT 21-SEP-2011, sequence version 1.
DT 24-JAN-2024, entry version 50.
DE RecName: Full=Chromosome partition protein Smc {ECO:0000256|HAMAP-Rule:MF_01894};
GN Name=smc {ECO:0000256|HAMAP-Rule:MF_01894};
GN ORFNames=AXXA_17106 {ECO:0000313|EMBL:EGP45112.1};
OS Achromobacter insuavis AXX-A.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae; Achromobacter.
OX NCBI_TaxID=1003200 {ECO:0000313|EMBL:EGP45112.1, ECO:0000313|Proteomes:UP000004853};
RN [1] {ECO:0000313|EMBL:EGP45112.1, ECO:0000313|Proteomes:UP000004853}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AXX-A {ECO:0000313|EMBL:EGP45112.1,
RC ECO:0000313|Proteomes:UP000004853};
RA Bador J., Amoureux L., Neuwirth C.;
RL Submitted (JUN-2011) 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:EGP45112.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AFRQ01000063; EGP45112.1; -; Genomic_DNA.
DR AlphaFoldDB; F7T3J6; -.
DR PATRIC; fig|1003200.3.peg.3396; -.
DR eggNOG; COG1196; Bacteria.
DR HOGENOM; CLU_001042_2_2_4; -.
DR Proteomes; UP000004853; 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; 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}.
FT DOMAIN 500..607
FT /note="SMC hinge"
FT /evidence="ECO:0000259|SMART:SM00968"
FT COILED 152..246
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 282..330
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 387..488
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 641..794
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 842..876
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 978..1005
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT BINDING 14..21
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
SQ SEQUENCE 1159 AA; 129023 MW; 139F9A3D36358304 CRC64;
MIPVPSQLVG VVGPNGCGKS NIIDAVRWVL GEAKASELRG ESMQDVIFNG SGNRKPAARA
SVEMVFDNSE GRAAGQWSTY AEIAVRRVLT RDGTSSYFVN NQQVRRRDIH DIFLGTGLGA
RGYAIIGQGM INRLIEARPE ELRVFLEEAA GVSRYKERRR ETENRLSDTR ENLTRVEDIL
RELNSQLEKL EAQAEVATRY RELQADGEKK QHALWFLKET GAREERARKT QEMAQAQNEL
EAAIAGLRAG EAALESRRQA HYAASDAVHT SQGALYEANA QVSRLEAEIR HVVDSRNRLQ
ARRDQLQQQI AEWTSQREHC TEQIAQAEED LAAGAARTEE ARAAAEDAQA ALPAVEQRVR
EAASGRDEMR ASLARVEQNL ALVAQTQRDA DRQMQTLEQR RERLQQELRE LHSPDPVRLE
QLAGDRVAGE DQLEEAQEAL ATLEGQVPDA DAERSRAQAA AQTDAQNLAR LEARLSALVK
LQEDVQKQGA LEPWLAKHEL AGLSRLWQKL HIEPGWETAL EAALRERMAS LEVRSLDWAR
AFSEDAPPAR LAFYQLPAAA PAPAAPAGLT PLASLLRITD PDLRTLLNDW LGGIYTATDL
AQALATRATL PAGAACVVKA GHLVDAHSVR FYAPDSEQAG LLARQQEIEN LQREIKAQQL
ITDQARAAVA RAEVAWQQVS QAIAPARQRV AEVTRRVHDI QLEHSRLQQQ AEQSGQHASR
LRQDLEEISA HEEDLRATRE EAEARFEALD EELAEHQSRF ADAEMDGETL AAQAEAARTR
LRELERAAQE AEFAERGIQV RITDLQRNRQ LAADQSQRGE VELEQLLADL VDLDASASQA
GLQDALELRA EREEALSRAR QEMENLAALL RGADEDRMQQ ERTLEPRRAR ITELQLQEQA
ARLAEEQFTE QLNAREVDRE ALAQDLANQP DEWRRASWLQ SEVTRISRQI ESLGSVNLAA
LDELNTSRER KGFLDDQHQD LMTAIETLED AIRKIDRETR DLLQETFNVV NGHFGELFPK
LFGGGEAKLT MTGEEILDAG VQVMAQPPGK RNSTIHLLSG GEKALTATAL VFALFKLNPA
PFCLLDEVDA PLDDANTERY ANLVANMSEQ TQFLFISHNK IAMQMAKQLI GVTMQEQGVS
RIVAVDIDSA VQMMASEAA
//
