ID F2JMX7_CELLD Unreviewed; 721 AA.
AC F2JMX7;
DT 31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 31-MAY-2011, sequence version 1.
DT 24-JAN-2024, entry version 47.
DE SubName: Full=Maltose O-acetyltransferase {ECO:0000313|EMBL:ADZ85892.1};
DE EC=2.3.1.79 {ECO:0000313|EMBL:ADZ85892.1};
GN OrderedLocusNames=Clole_4220 {ECO:0000313|EMBL:ADZ85892.1};
OS Cellulosilyticum lentocellum (strain ATCC 49066 / DSM 5427 / NCIMB 11756 /
OS RHM5) (Clostridium lentocellum).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Cellulosilyticaceae;
OC Cellulosilyticum.
OX NCBI_TaxID=642492 {ECO:0000313|EMBL:ADZ85892.1, ECO:0000313|Proteomes:UP000008467};
RN [1] {ECO:0000313|EMBL:ADZ85892.1, ECO:0000313|Proteomes:UP000008467}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49066 / DSM 5427 / NCIMB 11756 / RHM5
RC {ECO:0000313|Proteomes:UP000008467};
RX PubMed=21398547; DOI=10.1128/JB.00239-11;
RG US DOE Joint Genome Institute;
RA Miller D.A., Suen G., Bruce D., Copeland A., Cheng J.F., Detter C.,
RA Goodwin L.A., Han C.S., Hauser L.J., Land M.L., Lapidus A., Lucas S.,
RA Meincke L., Pitluck S., Tapia R., Teshima H., Woyke T., Fox B.G.,
RA Angert E.R., Currie C.R.;
RT "Complete genome sequence of the cellulose-degrading bacterium
RT Cellulosilyticum lentocellum.";
RL J. Bacteriol. 193:2357-2358(2011).
CC -!- SIMILARITY: Belongs to the transferase hexapeptide repeat family.
CC {ECO:0000256|ARBA:ARBA00007274}.
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DR EMBL; CP002582; ADZ85892.1; -; Genomic_DNA.
DR AlphaFoldDB; F2JMX7; -.
DR STRING; 642492.Clole_4220; -.
DR KEGG; cle:Clole_4220; -.
DR eggNOG; COG0110; Bacteria.
DR eggNOG; COG0456; Bacteria.
DR eggNOG; COG3064; Bacteria.
DR HOGENOM; CLU_383436_0_0_9; -.
DR Proteomes; UP000008467; Chromosome.
DR GO; GO:0008925; F:maltose O-acetyltransferase activity; IEA:UniProtKB-EC.
DR CDD; cd03357; LbH_MAT_GAT; 1.
DR CDD; cd04301; NAT_SF; 1.
DR Gene3D; 3.40.630.30; -; 1.
DR Gene3D; 2.160.10.10; Hexapeptide repeat proteins; 1.
DR InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR InterPro; IPR000182; GNAT_dom.
DR InterPro; IPR001451; Hexapep.
DR InterPro; IPR039369; LacA-like.
DR InterPro; IPR024688; Mac_dom.
DR InterPro; IPR011004; Trimer_LpxA-like_sf.
DR PANTHER; PTHR43017:SF1; ACETYLTRANSFERASE YJL218W-RELATED; 1.
DR PANTHER; PTHR43017; GALACTOSIDE O-ACETYLTRANSFERASE; 1.
DR Pfam; PF00583; Acetyltransf_1; 1.
DR Pfam; PF00132; Hexapep; 1.
DR Pfam; PF12464; Mac; 1.
DR SMART; SM01266; Mac; 1.
DR SUPFAM; SSF55729; Acyl-CoA N-acyltransferases (Nat); 1.
DR SUPFAM; SSF51161; Trimeric LpxA-like enzymes; 1.
DR PROSITE; PS51186; GNAT; 1.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000256|ARBA:ARBA00023315,
KW ECO:0000313|EMBL:ADZ85892.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000008467};
KW Transferase {ECO:0000313|EMBL:ADZ85892.1}.
FT DOMAIN 3..162
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS51186"
FT REGION 186..360
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 430..480
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 721 AA; 84642 MW; 1221576CA2FEEF31 CRC64;
MELTIRRALA TDALFLTSIS FGAKRYWNYP EEYFEVWHDE LTITEDYIEQ NIVYVAQKKD
TIIGYFSIVE VNQEHWNGEV FISRGYWLDH IYIRPAYIRS GIGTELMEYA QEYCRENGIE
KLYIFSDPFA NGFYEKLGAT YIKESPSSIE NRTVSLYEYR IPEKSKEQIE EEELLQKIQE
EAERLRQEAE EAEEAERLRQ EAEEAERLRQ EAEEAERLRQ EAEEAERLRQ EAEEAERLRQ
EAEEAERLRQ EAEEAERLRQ EAEEAERLRQ EAEEAERLRQ EAEEAERLRQ EAEEAERLRQ
EAEEAERLRQ EAEEAERLRQ EAEEAERLRQ EAERLRQEAE EAERLRQEAE EAERLRQEAE
ETERLIQEAE KAREILQEED AKQKRKSIFG IPIEKIKHRP IKLEHESLEQ KISELDQEFE
DDFEDIEEVA EEATLYEIDE SEEYDEDHEE YSDNEDDEDY SDDEDDEDYS DYEDDEEYAE
DELIEDDREI QIPKLQLDEA EIAALIRPVK DDASEEEKIL ENIRTASTEI EVHIKTEKEK
MLAGELYIAW GDEFANDKRR ARRLLREFNN TDVEDKKATI KILKELFGST GEYIHIEPNF
RCDYGYNIHI GDNFYAGYEC VILDSCQVKI GDNCILSPQV GIYTSAYPLN PEKRSIGYEY
AKPITIGNNV WIGGGSIINP GVTIGDNVVV VPGSVVLADV PDNVLIGGNP AKVIKEIETE
K
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