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Database: UniProt
Entry: A8HT58_AZOC5
LinkDB: A8HT58_AZOC5
Original site: A8HT58_AZOC5 
ID   A8HT58_AZOC5            Unreviewed;      1150 AA.
AC   A8HT58;
DT   04-DEC-2007, integrated into UniProtKB/TrEMBL.
DT   04-DEC-2007, sequence version 1.
DT   27-MAR-2024, entry version 90.
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:BAF90256.1};
GN   OrderedLocusNames=AZC_4258 {ECO:0000313|EMBL:BAF90256.1};
OS   Azorhizobium caulinodans (strain ATCC 43989 / DSM 5975 / JCM 20966 / LMG
OS   6465 / NBRC 14845 / NCIMB 13405 / ORS 571).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Xanthobacteraceae; Azorhizobium.
OX   NCBI_TaxID=438753 {ECO:0000313|EMBL:BAF90256.1, ECO:0000313|Proteomes:UP000000270};
RN   [1] {ECO:0000313|EMBL:BAF90256.1, ECO:0000313|Proteomes:UP000000270}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43989 / DSM 5975 / JCM 20966 / LMG 6465 / NBRC 14845 /
RC   NCIMB 13405 / ORS 571 {ECO:0000313|Proteomes:UP000000270};
RX   PubMed=17720818; DOI=10.1128/AEM.01514-07;
RA   Suzuki S., Aono T., Lee KB., Suzuki T., Liu CT., Miwa H., Wakao S., Iki T.,
RA   Oyaizu H.;
RT   "Rhizobial factors required for stem nodule maturation and maintenance in
RT   Sesbania rostrata-Azorhizobium caulinodans ORS571 symbiosis.";
RL   Appl. Environ. Microbiol. 73:6650-6659(2007).
RN   [2] {ECO:0000313|Proteomes:UP000000270}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43989 / DSM 5975 / JCM 20966 / LMG 6465 / NBRC 14845 /
RC   NCIMB 13405 / ORS 571 {ECO:0000313|Proteomes:UP000000270};
RA   Lee K.B., Backer P.D., Aono T., Liu C.T., Suzuki S., Suzuki T., Kaneko T.,
RA   Yamada M., Tabata S., Kupfer D.M., Najar F.Z., Wiley G.B., Roe B.,
RA   Binnewies T., Ussery D., Vereecke D., Gevers D., Holsters M., Oyaizu H.;
RT   "Complete genome sequence of the nitrogen-fixing bacterium Azorhizobium
RT   caulinodans ORS571.";
RL   Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EMBL:BAF90256.1, ECO:0000313|Proteomes:UP000000270}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43989 / DSM 5975 / JCM 20966 / LMG 6465 / NBRC 14845 /
RC   NCIMB 13405 / ORS 571 {ECO:0000313|Proteomes:UP000000270};
RX   PubMed=18522759; DOI=10.1186/1471-2164-9-271;
RA   Lee KB., Backer P.D., Aono T., Liu CT., Suzuki S., Suzuki T., Kaneko T.,
RA   Yamada M., Tabata S., Kupfer D.M., Najar F.Z., Wiley G.B., Roe B.,
RA   Binnewies T.T., Ussery D.W., D'Haeze W., Herder J.D., Gevers D.,
RA   Vereecke D., Holsters M., Oyaizu H.;
RT   "The genome of the versatile nitrogen fixer Azorhizobium caulinodans
RT   ORS571.";
RL   BMC Genomics 9:271-271(2008).
RN   [4] {ECO:0000313|EMBL:BAF90256.1, ECO:0000313|Proteomes:UP000000270}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43989 / DSM 5975 / JCM 20966 / LMG 6465 / NBRC 14845 /
RC   NCIMB 13405 / ORS 571 {ECO:0000313|Proteomes:UP000000270};
RX   PubMed=19542345; DOI=10.1128/AEM.00398-09;
RA   Tsukada S., Aono T., Akiba N., Lee KB., Liu CT., Toyazaki H., Oyaizu H.;
RT   "Comparative genome-wide transcriptional profiling of Azorhizobium
RT   caulinodans ORS571 grown under free-living and symbiotic conditions.";
RL   Appl. Environ. Microbiol. 75:5037-5046(2009).
RN   [5] {ECO:0000313|EMBL:BAF90256.1, ECO:0000313|Proteomes:UP000000270}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43989 / DSM 5975 / JCM 20966 / LMG 6465 / NBRC 14845 /
RC   NCIMB 13405 / ORS 571 {ECO:0000313|Proteomes:UP000000270};
RX   PubMed=20382809; DOI=10.1128/AEM.00238-10;
RA   Akiba N., Aono T., Toyazaki H., Sato S., Oyaizu H.;
RT   "phrR-like gene praR of Azorhizobium caulinodans ORS571 is essential for
RT   symbiosis with Sesbania rostrata and is involved in expression of reb
RT   genes.";
RL   Appl. Environ. Microbiol. 76:3475-3485(2010).
RN   [6] {ECO:0000313|EMBL:BAF90256.1, ECO:0000313|Proteomes:UP000000270}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43989 / DSM 5975 / JCM 20966 / LMG 6465 / NBRC 14845 /
RC   NCIMB 13405 / ORS 571 {ECO:0000313|Proteomes:UP000000270};
RX   PubMed=21571889; DOI=10.1128/AEM.02327-10;
RA   Liu CT., Lee KB., Wang YS., Peng MH., Lee KT., Suzuki S., Suzuki T.,
RA   Oyaizu H.;
RT   "Involvement of the azorhizobial chromosome partition gene (parA) in the
RT   onset of bacteroid differentiation during Sesbania rostrata stem nodule
RT   development.";
RL   Appl. Environ. Microbiol. 77:4371-4382(2011).
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; AP009384; BAF90256.1; -; Genomic_DNA.
DR   RefSeq; WP_012172778.1; NC_009937.1.
DR   AlphaFoldDB; A8HT58; -.
DR   STRING; 438753.AZC_4258; -.
DR   KEGG; azc:AZC_4258; -.
DR   eggNOG; COG1196; Bacteria.
DR   HOGENOM; CLU_001042_2_2_5; -.
DR   Proteomes; UP000000270; 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; 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   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; 2.
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:UP000000270}.
FT   DOMAIN          505..593
FT                   /note="SMC hinge"
FT                   /evidence="ECO:0000259|SMART:SM00968"
FT   COILED          170..211
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT   COILED          289..472
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT   COILED          635..773
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT   COILED          858..988
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   1150 AA;  125463 MW;  BA32F206CD07CDB2 CRC64;
     MKFNRLRLVG FKTFVEPTDL LIEPGLTGVV GPNGCGKSNL VEALRWVMGE SSHKAFRAND
     MDDVIFSGTT GRPARNTAEV ALQLDNAERT APAGFNDHDL IEVVRRIDRG QGSHYRINGR
     DVRARDVNML FADASTGARS PALVRQGQIG EIVGAKPAAR RRILEEAAGV AGLHARRHEA
     ETRLKAAETN LLRLEDVITQ LAGQVEGLRR QARQAVRYRA LAAEIRKYEA TLLWLRWSEV
     TRTLADAERT LEASVREAAE CTRAQAEAAR LQAIAAHALP ALRQADTEAA AALQRLTLAR
     VELDKEEERL GARRLDLERR LAQLTQDLER ETALSADAEG VLARLEEEEL TLTEEQEASV
     LAREEAEAIL DTAQEAMAAA EDDLDAKTRA YADASARRTT LDQTIRDIRQ RLLRTEAERV
     SVEAEERRLK LDAGTSDLEA KRMEADAARE RLAFAEEAAT DAEAAHQSAR RALEEVRPAV
     AEAERKFGRL DTEVRTLSKL LQSSSGAFPP VADLLTVTKG YEMALGAALG DDLDLPVDTA
     APARWAGSQP QAGDPALPPG AGPLADEVSG APALLRRLGQ IGIVEPADGP RLQAQLKPGQ
     RLVSKAGDLW RWDGVIAAAD APTAAARRLA ERNRLADLQL EADLAREAVE EARDMLALRD
     ADLRAAAGLE TQAREARRTA QRAAEIAREA EANAERKASA HIARLSALTE ARERLTAARA
     EAEERLAEAE ASLAELEQPA LIDATLAAAR GVVAQARGAV AEAKARLDGF ERERSQRLRR
     LEAIASERRS WTSRAGGAGE RLAAIAARKA ETETELATTE EMPAQFLFQR RTLLGKIEAA
     DEARRAAADK LVEGESALAA ADRAARAALE AMSAAREETA RAEARLDAAR QRRDDVQREI
     TEALDGPPES AREHAELVDD GRQPDISAIE IALERAKRER ERLGAVNLRA EIELTETETQ
     HDTLVRERDE LNEAIRRLRG AIASLNREAR ERLQASFAVV DGHFRKLFDT LFGGGEAQLV
     LTDADDPLEA GLDIIAKPPG KKPQSLSLLS GGEQALTAMA LIFAVFLTNP APICVLDEVD
     APLDDSNVER FCTLMDEMTR LTDTRFLVIT HNPISMAHMD RLFGVTMAER GVSRLVSVDL
     QSAERLREVS
//
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