ID M6ZPT1_LEPIR Unreviewed; 418 AA.
AC M6ZPT1;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 24-JAN-2024, entry version 37.
DE RecName: Full=3-deoxy-D-manno-octulosonic acid transferase {ECO:0000256|RuleBase:RU365103};
DE Short=Kdo transferase {ECO:0000256|RuleBase:RU365103};
DE EC=2.4.99.12 {ECO:0000256|RuleBase:RU365103};
DE AltName: Full=Lipid IV(A) 3-deoxy-D-manno-octulosonic acid transferase {ECO:0000256|RuleBase:RU365103};
GN Name=waaA {ECO:0000313|EMBL:EMP08071.1};
GN ORFNames=LEP1GSC124_1856 {ECO:0000313|EMBL:EMP08071.1};
OS Leptospira interrogans serovar Pyrogenes str. 200701872.
OC Bacteria; Spirochaetota; Spirochaetia; Leptospirales; Leptospiraceae;
OC Leptospira.
OX NCBI_TaxID=1193029 {ECO:0000313|EMBL:EMP08071.1, ECO:0000313|Proteomes:UP000012117};
RN [1] {ECO:0000313|EMBL:EMP08071.1, ECO:0000313|Proteomes:UP000012117}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=200701872 {ECO:0000313|EMBL:EMP08071.1,
RC ECO:0000313|Proteomes:UP000012117};
RA Harkins D.M., Durkin A.S., Brinkac L.M., Haft D.H., Selengut J.D.,
RA Sanka R., DePew J., Purushe J., Picardeau M., Werts C., Goarant C.,
RA Vinetz J.M., Sutton G.G., Nierman W.C., Fouts D.E.;
RL Submitted (JAN-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Involved in lipopolysaccharide (LPS) biosynthesis. Catalyzes
CC the transfer of 3-deoxy-D-manno-octulosonate (Kdo) residue(s) from CMP-
CC Kdo to lipid IV(A), the tetraacyldisaccharide-1,4'-bisphosphate
CC precursor of lipid A. {ECO:0000256|RuleBase:RU365103}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=CMP-3-deoxy-beta-D-manno-octulosonate + lipid IVA (E. coli) =
CC alpha-Kdo-(2->6)-lipid IVA (E. coli) + CMP + H(+);
CC Xref=Rhea:RHEA:28066, ChEBI:CHEBI:15378, ChEBI:CHEBI:58603,
CC ChEBI:CHEBI:60364, ChEBI:CHEBI:60377, ChEBI:CHEBI:85987;
CC EC=2.4.99.12; Evidence={ECO:0000256|RuleBase:RU365103};
CC -!- PATHWAY: Bacterial outer membrane biogenesis; LPS core biosynthesis.
CC {ECO:0000256|RuleBase:RU365103}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|RuleBase:RU365103}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase group 1 family.
CC {ECO:0000256|RuleBase:RU365103}.
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:EMP08071.1}.
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DR EMBL; AKWN02000167; EMP08071.1; -; Genomic_DNA.
DR AlphaFoldDB; M6ZPT1; -.
DR UniPathway; UPA00958; -.
DR Proteomes; UP000012117; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0043842; F:Kdo transferase activity; IEA:UniProtKB-EC.
DR GO; GO:0009244; P:lipopolysaccharide core region biosynthetic process; IEA:UniProtKB-UniRule.
DR Gene3D; 3.40.50.11720; 3-Deoxy-D-manno-octulosonic-acid transferase, N-terminal domain; 1.
DR Gene3D; 3.40.50.2000; Glycogen Phosphorylase B; 1.
DR InterPro; IPR007507; Glycos_transf_N.
DR InterPro; IPR038107; Glycos_transf_N_sf.
DR InterPro; IPR039901; Kdotransferase.
DR PANTHER; PTHR42755:SF1; 3-DEOXY-D-MANNO-OCTULOSONIC ACID TRANSFERASE, MITOCHONDRIAL-RELATED; 1.
DR PANTHER; PTHR42755; 3-DEOXY-MANNO-OCTULOSONATE CYTIDYLYLTRANSFERASE; 1.
DR Pfam; PF04413; Glycos_transf_N; 1.
PE 3: Inferred from homology;
KW Cell membrane {ECO:0000256|RuleBase:RU365103};
KW Lipopolysaccharide biosynthesis {ECO:0000256|RuleBase:RU365103};
KW Membrane {ECO:0000256|RuleBase:RU365103};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU365103};
KW Transmembrane {ECO:0000256|RuleBase:RU365103};
KW Transmembrane helix {ECO:0000256|RuleBase:RU365103}.
FT TRANSMEM 6..30
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365103"
FT DOMAIN 47..208
FT /note="3-deoxy-D-manno-octulosonic-acid transferase N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF04413"
FT ACT_SITE 62
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR639901-1"
SQ SEQUENCE 418 AA; 47737 MW; 334B992347F96BB8 CRC64;
MIFLYQILTI FLLIFVVPIS FLFPSARLFF RKRSADKKKI LSKSLDLSGK YTVWLHAASV
GELDQCKALA LEFRKNDPSA FLIQSVFSDS VRDSQLEAFP ADETFHLPID LPFSYDWIFS
RFHPKVLVLM AWDTWPNLVI SANRFNTKVV LGSAVIGNRK KGIMGKLTKS VFKHLDGIFP
SHESFYDVFR SLVPDQIPVK VLGDTRFDSV LKKIEDNAKI FKKPKNYPYS KIILFASTYE
PCENLIVSLY ELIRSKNPAL LDNFAFWIFP HKTSPDRIIS IEHKLQDANI IYQTWTSTPF
ENLTAQTIVF DVLGVLAFAY QAADFAYVGG ALHNRVHNIL EPATFGLPLM TGPKIYNSPE
AMILEKSGGL FIVSKAEDIF QILNLSENDL ETIRKQNWEF VQSGRGAAKR LYEEIRKL
//
