ID A0A0F4QFU3_9GAMM Unreviewed; 1135 AA.
AC A0A0F4QFU3;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 24-JAN-2024, entry version 28.
DE RecName: Full=Chromosome partition protein Smc {ECO:0000256|HAMAP-Rule:MF_01894};
GN Name=smc {ECO:0000256|HAMAP-Rule:MF_01894};
GN ORFNames=TW77_19185 {ECO:0000313|EMBL:KJZ06451.1};
OS Pseudoalteromonas rubra.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Pseudoalteromonadaceae; Pseudoalteromonas.
OX NCBI_TaxID=43658 {ECO:0000313|EMBL:KJZ06451.1, ECO:0000313|Proteomes:UP000033452};
RN [1] {ECO:0000313|EMBL:KJZ06451.1, ECO:0000313|Proteomes:UP000033452}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S2471 {ECO:0000313|EMBL:KJZ06451.1,
RC ECO:0000313|Proteomes:UP000033452};
RX PubMed=25879706; DOI=10.1186/s12864-015-1365-z;
RA Machado H., Sonnenschein E.C., Melchiorsen J., Gram L.;
RT "Genome mining reveals unlocked bioactive potential of marine Gram-negative
RT bacteria.";
RL BMC Genomics 16:158-158(2015).
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:KJZ06451.1}.
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DR EMBL; JXYA01000049; KJZ06451.1; -; Genomic_DNA.
DR RefSeq; WP_046006592.1; NZ_JXYA01000049.1.
DR AlphaFoldDB; A0A0F4QFU3; -.
DR PATRIC; fig|43658.5.peg.4052; -.
DR OrthoDB; 9808768at2; -.
DR Proteomes; UP000033452; 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 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; 1.
DR PIRSF; PIRSF005719; SMC; 2.
DR SUPFAM; SSF90257; Myosin rod fragments; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
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};
KW Reference proteome {ECO:0000313|Proteomes:UP000033452}.
FT DOMAIN 3..1119
FT /note="RecF/RecN/SMC N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02463"
FT REGION 750..780
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 170..218
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 244..411
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 452..500
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 832..880
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 943..977
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COMPBIAS 753..780
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 32..39
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
SQ SEQUENCE 1135 AA; 126965 MW; DF757E4FEDC3C7C9 CRC64;
MRLSSIKLAG FKSFVEPTKI PFPEPMTCVV GPNGCGKSNV IDAVRWVLGE SSAKNLRGDA
MTDVIFNGST HRKPVSQASV ELLFDNTQGR LPGSMADRTQ VAIKRLVTRD GQSLYFLNGS
KCRKRDITDI FLGTGLGPRS YAIIEQGMIS RLIESKPQEL RIFLEEAAGV SKYKERRRET
QTRIKSTREN LERLLDMRQE LQNQLDRLAK QAEAARQYRD LKAQERTLKG QLAVLKWQEL
HAKQQEKTTQ IAKLNEQLTF LEQAHGGHDD VLASFEQQVT HFSDAQAALQ QQLHSTQTQL
TRIEQQKIHL SEKRRELADK HTQLNEEIAQ AQALYEQQQQ HCAELVELCE AHQEATQISA
EKLAEAELLI DEKMQQLQTY EASSQTAQRA LEKVRQHTQQ CQLALQRLTQ QQQHQSQRQA
QLVQQQAQHS AQNPAEMLAE QQKAHQELVH AMAISQQENQ RLSAELQRLS EARTALQNKC
QAQQVRLGQA QAQVQALEKL TRAQQGDSQD APGEPLLSVL RAEPGLEAIV ERAMFGLGSL
RITEQDYASR IWPAPEGEKT PGSVATLVQS EIYPDFLNQI EWLGQARHFS ARGAFFAAID
DEGTLYGGNW QAQEEDAQSG SLLAHYSELR GHKTALPQIE AQLSELEASL TPLESAVTTC
SQQLEANKQA VHEAAKQVAS SQTRVDMLLA QQASWQQQSS QLERSQRELD EQGELLVAQL
EESEQALWQA EEAQEQLQQQ MNQAGEALEA LKRAHQQQQQ QQRDIQQQHH QAKMKLQQAQ
SDAQLGQTKL SHLAQSLKLG TEALDQVQQQ LSSCDEPGVE LEQQQTELLI RHTELEQAAK
ETAAKLSDAK QQLADKQLAL KDAQAKSTQL KEQRQQLALQ EQSLMVKAQA VLEPLTELRQ
TLKDVLAQLP EDAQASSHQG KLTRIGQLLS LLGAVNLAAI EEFDEAQQRK RYLDEQLDDL
SAALETLEGA IRKIDRETRS RFKTTFDQVN QGLAELFPKV FGGGSAYLEL TSDDLLESGV
SIMARPPGKK NSTIHLLSGG EKALTALSLV FSIFRLNPAP FCMLDEVDAP LDDANVGRFC
RLVEEMSQTV QFIYISHNKV AMEMAGRLTG VTMAEPGVSR MVAVDIEQAV QMAHA
//
