ID H3ZHY7_9ALTE Unreviewed; 1137 AA.
AC H3ZHY7;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 24-JAN-2024, entry version 43.
DE RecName: Full=Chromosome partition protein Smc {ECO:0000256|HAMAP-Rule:MF_01894};
GN Name=smc {ECO:0000256|HAMAP-Rule:MF_01894};
GN ORFNames=AJE_14975 {ECO:0000313|EMBL:EHR39993.1};
OS Alishewanella jeotgali KCTC 22429.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Alteromonadaceae; Alishewanella.
OX NCBI_TaxID=1129374 {ECO:0000313|EMBL:EHR39993.1, ECO:0000313|Proteomes:UP000012046};
RN [1] {ECO:0000313|EMBL:EHR39993.1, ECO:0000313|Proteomes:UP000012046}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KCTC 22429 {ECO:0000313|EMBL:EHR39993.1,
RC ECO:0000313|Proteomes:UP000012046};
RX PubMed=22461542; DOI=10.1128/JB.00153-12;
RA Jung J., Chun J., Park W.;
RT "Genome Sequence of Extracellular-Protease-Producing Alishewanella jeotgali
RT Isolated from Traditional Korean Fermented Seafood.";
RL J. Bacteriol. 194:2097-2097(2012).
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. {ECO:0000256|HAMAP-
CC Rule:MF_01894}.
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:EHR39993.1}.
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DR EMBL; AHTH01000048; EHR39993.1; -; Genomic_DNA.
DR RefSeq; WP_008951545.1; NZ_AHTH01000048.1.
DR AlphaFoldDB; H3ZHY7; -.
DR STRING; 1129374.AJE_14975; -.
DR PATRIC; fig|1129374.4.peg.2966; -.
DR eggNOG; COG1196; Bacteria.
DR Proteomes; UP000012046; Unassembled WGS sequence.
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; 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; PF02463; SMC_N; 2.
DR PIRSF; PIRSF005719; SMC; 2.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|HAMAP-Rule:MF_01894};
KW Coiled coil {ECO:0000256|HAMAP-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 3..138
FT /note="RecF/RecN/SMC N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02463"
FT DOMAIN 814..1121
FT /note="RecF/RecN/SMC N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02463"
FT COILED 170..218
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 244..383
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 431..486
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 631..861
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 1137 AA; 128670 MW; 268827834BFEC232 CRC64;
MRLKQIKLAG FKSFVDPTTV PFPQAMTAIV GPNGCGKSNV IDAVRWVLGE SSAKNLRGDA
MTDVIFNGSA QRKPVSQASV ELVFENTQGR LAGNLADRSE IAIKRVVTRD AQSLYFLNGS
KCRRRDITDI FLGTGLGPRS YAIIEQGMIS RLIESKPQEL RVFIEEAAGI SRYKERRRET
ENRIKHTRDN LDRLTDVREE LGKNIDKLKR QAATAQRYKE LKAQERTLRA QLTTIKWLGF
NDTLNKLEQQ LREQETELQK YQAAQAGDER VLTELREQAN TARQQQEQCQ QQYYQLGNRI
SALEQQIVGQ RQQQQLLSQQ IQQKQLSLAG FHEQQQQEQL QRAELEAQLE ELIPELLLLT
EQQEELQAQL LEATEQAAET QLNWQDWQQQ HYQRREQLQQ WRLQLQHWAQ QQHQLAAQQH
KLTEQLARLE PEQAEQELAL AEARHQELAE QVAALQLEQA ELTAALAQQQ QLSAQATQQR
QQWQNQQQVL RIEHQRLSHS QQQASSSGPL LAEQLQIADG WALAVTLALG ALQQAELAAH
TAGKALYVIA TAGDNAAPAN TLASVVRSGV YPDYFRQILL AADEAQALTM LTQLKPGQSV
ICAKGKWFGT NWGQQSQASL TDSRLLRQER LQQLGQELAV VEQELAAAAA AEQQQLELQQ
QAQQQLSQLN AALSSQQQAR QQQHTVVQLK QQALQQLRQQ STQLQQQLAE LQLQQQALAA
SAEQTELKLA EAEQEYQQAV TQEQQLQQRQ QQARAQEETL RQQLQQQQGQ HSQLQMQQRL
CQQQLQSVEL SLSRAALQQQ QWLEQLAELQ LQLDEQQDPA LQLQEELQES LLQRSDAEQA
LTNANQQLAA IQQQIRELEQ GQSGITQRLS SQQKALENLR LDAEGYRIRA NNMLELLREQ
QVNMKEVLAE LPADADEAQW QQQLDKTVEA VSRLGAINLA AIEEYEQQAE RKAYLDAQHQ
DLTSALDTLE TAIRKIDRET RQRFKETFDQ VNDGLKQLFP KVFGGGSAYL DLTDDDLLET
GVSIMARPPG KKNSTIHLLS GGEKALTALS LVFSIFRLNP APFCMLDEVD APLDDANVGR
FCNLVREMSD TVQFIYISHN KIAMEMAAQL MGVTMQEPGV SRVVAVDVDD AVKLAVA
//
