ID G7ZFB7_AZOL4 Unreviewed; 1153 AA.
AC G7ZFB7;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 27-MAR-2024, entry version 56.
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:CBS90172.1};
GN OrderedLocusNames=AZOLI_p30343 {ECO:0000313|EMBL:CBS90172.1};
OS Azospirillum lipoferum (strain 4B).
OG Plasmid AZO_p3 {ECO:0000313|EMBL:CBS90172.1,
OG ECO:0000313|Proteomes:UP000005667}.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Azospirillaceae; Azospirillum.
OX NCBI_TaxID=862719 {ECO:0000313|EMBL:CBS90172.1, ECO:0000313|Proteomes:UP000005667};
RN [1] {ECO:0000313|Proteomes:UP000005667}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=4B {ECO:0000313|Proteomes:UP000005667};
RC PLASMID=Plasmid AZO_p3 {ECO:0000313|Proteomes:UP000005667};
RX PubMed=22216014; DOI=10.1371/journal.pgen.1002430;
RA Wisniewski-Dye F., Borziak K., Khalsa-Moyers G., Alexandre G.,
RA Sukharnikov L.O., Wuichet K., Hurst G.B., McDonald W.H., Robertson J.S.,
RA Barbe V., Calteau A., Rouy Z., Mangenot S., Prigent-Combaret C.,
RA Normand P., Boyer M., Siguier P., Dessaux Y., Elmerich C., Condemine G.,
RA Krishnen G., Kennedy I., Paterson A.H., Gonzalez V., Mavingui P.,
RA Zhulin I.B.;
RT "Azospirillum genomes reveal transition of bacteria from aquatic to
RT terrestrial environments.";
RL PLoS Genet. 7:E1002430-E1002430(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 Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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. {ECO:0000256|HAMAP-
CC Rule:MF_01894}.
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DR EMBL; FQ311871; CBS90172.1; -; Genomic_DNA.
DR RefSeq; WP_014249613.1; NC_016623.1.
DR AlphaFoldDB; G7ZFB7; -.
DR KEGG; ali:AZOLI_p30343; -.
DR HOGENOM; CLU_001042_2_2_5; -.
DR OrthoDB; 9808768at2; -.
DR Proteomes; UP000005667; Plasmid AZO_p3.
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; 1.10.287.1490; -; 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; IPR036277; SMC_hinge_sf.
DR InterPro; IPR011890; SMC_prok.
DR NCBIfam; TIGR02168; SMC_prok_B; 1.
DR PANTHER; PTHR18937; STRUCTURAL MAINTENANCE OF CHROMOSOMES SMC FAMILY MEMBER; 1.
DR Pfam; PF02463; SMC_N; 1.
DR PIRSF; PIRSF005719; SMC; 2.
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 Plasmid {ECO:0000313|EMBL:CBS90172.1}.
FT DOMAIN 4..1136
FT /note="RecF/RecN/SMC N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02463"
FT REGION 457..482
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 289..323
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 631..707
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 805..881
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 950..991
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 1153 AA; 124570 MW; D0A9AC50167BE340 CRC64;
MQFTRLRLSG FKSFVDATEL VIEPGMTGIV GPNGCGKSNL VEALRWVMGE TSAKRMRGGD
MDDVIFGGTS SRPARNLGEV TLAVDNRSRT APAGFNEHDE LEITRRIERG SGSDYRINGK
LVRARDVQLL FADNASGAAS PALVSQGKVA QIISAKPQDR RALLEEAAGI TGLHSRRHEA
ELRLKAAEGN LTRLDDVIGA MDTQLQSLKK QARQASRYRN LSDQIRKAEA VLWHLRWIAA
QEERARAHAA FAAAEAAVRD RMLSVNQLAA RRTEAAAGLP EKRQDEARAA SALQRLVIAR
EQLDAEEKRV ADQQRALEAR LRQIAGDLGR EEALAADAGE ALARLVAERD RLIAAQADEE
MLEDAAAEAL AEAREQVDAL DRELTRLTEE VATDEARRAA TQRQAAELET RAAGLAKRLA
EQQAQRAALE AEIAARADLS DAELAVELAE QRLEQAREAA EAAEQAKAEA EPAQSRAREA
LSAAESARAK LHAEERALAE LLEAGAGGPF PPLVDAVAVS PGYEGALAAA LGDALTAPLD
EEAPVHWRTL PAYDSVAPLP DGVEPLSRHV EGPRAAARAL AHVGVVDDAA AAGVLAAALV
PGQVLVSRDG GAWRWDGLTV QAGAPTAAAV RLKQRNRLAE LRGELELAEE RVELARETLD
AAKLAVEAAA QADRRARDAV REGFAALNAA RDRHAKLARE ADAASSRLAA LVEAVERLAA
DEREAAARRD EALELLESLP DPREGRERVN DQRAALAERR AVLAERQNAV DRLTREAQAR
RHRLGAIQAE TTSWDSRSAG AGGRVAELRQ RAEEAEGELA QLSGRPAEIA AERQDLLNRI
TMAERDRKRA ADGLAEAEAR LAETEQALHD AEAALADGRE ARAHAEAAVS AALQQERTLT
ERIAERLDCR PEDTRAAADL DPAEPMPDAG AVEARLDKLT RERENMGPVN LRAEIEAQEL
EAQITGLHSE REDLTAAIAR LRQGIASLNR EARERLVASF DVVNRDFQEL FTRLFGGGKA
YLELVNAEDP LNAGLEIYAS PPGKKLQVLS LLSGGEQALT ALSLLFAVFR SNPAPICVLD
EVDAPLDEAN VGRFCDLVED IARQGDTRFL IITHHRLTMA RVDRLFGVTM VERGVSQLVS
VDLSAAEELR GVA
//
