GenomeNet

Database: UniProt
Entry: E7ABH8_HELFC
LinkDB: E7ABH8_HELFC
Original site: E7ABH8_HELFC 
ID   E7ABH8_HELFC            Unreviewed;       341 AA.
AC   E7ABH8;
DT   08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT   08-MAR-2011, sequence version 1.
DT   27-MAR-2024, entry version 59.
DE   RecName: Full=Probable endolytic peptidoglycan transglycosylase RlpA {ECO:0000256|HAMAP-Rule:MF_02071};
DE            EC=4.2.2.- {ECO:0000256|HAMAP-Rule:MF_02071};
GN   Name=rlpA {ECO:0000256|HAMAP-Rule:MF_02071,
GN   ECO:0000313|EMBL:CBY82857.1};
GN   OrderedLocusNames=Hfelis_07730 {ECO:0000313|EMBL:CBY82857.1};
OS   Helicobacter felis (strain ATCC 49179 / NCTC 12436 / CS1).
OC   Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC   Helicobacteraceae; Helicobacter.
OX   NCBI_TaxID=936155 {ECO:0000313|EMBL:CBY82857.1, ECO:0000313|Proteomes:UP000007934};
RN   [1] {ECO:0000313|Proteomes:UP000007934}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49179 / NCTC 12436 / CS1
RC   {ECO:0000313|Proteomes:UP000007934};
RA   Arnold A., Zigova Z., Lawley T., Falkow S., Bentley S., Aslett M.,
RA   Muller A.;
RT   "Comparative whole genome analysis of the carcinogenic bacterial pathogen
RT   Helicobacter felis.";
RL   Submitted (DEC-2010) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:CBY82857.1, ECO:0000313|Proteomes:UP000007934}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49179 / NCTC 12436 / CS1
RC   {ECO:0000313|Proteomes:UP000007934};
RX   PubMed=21402865;
RA   Arnold I.C., Zigova Z., Holden M., Lawley T.D., Rad R., Dougan G.,
RA   Falkow S., Bentley S.D., Muller A.;
RT   "Comparative whole genome sequence analysis of the carcinogenic bacterial
RT   model pathogen Helicobacter felis.";
RL   Genome Biol. Evol. 3:302-308(2011).
CC   -!- FUNCTION: Lytic transglycosylase with a strong preference for naked
CC       glycan strands that lack stem peptides. {ECO:0000256|HAMAP-
CC       Rule:MF_02071}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|HAMAP-Rule:MF_02071};
CC       Lipid-anchor {ECO:0000256|HAMAP-Rule:MF_02071}.
CC   -!- SIMILARITY: Belongs to the RlpA family. {ECO:0000256|HAMAP-
CC       Rule:MF_02071, ECO:0000256|RuleBase:RU003495}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; FQ670179; CBY82857.1; -; Genomic_DNA.
DR   AlphaFoldDB; E7ABH8; -.
DR   STRING; 936155.HFELIS_07730; -.
DR   KEGG; hfe:HFELIS_07730; -.
DR   eggNOG; COG0797; Bacteria.
DR   HOGENOM; CLU_042923_3_4_7; -.
DR   OrthoDB; 9779128at2; -.
DR   Proteomes; UP000007934; Chromosome.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0008932; F:lytic endotransglycosylase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0042834; F:peptidoglycan binding; IEA:InterPro.
DR   GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR   GO; GO:0000270; P:peptidoglycan metabolic process; IEA:UniProtKB-UniRule.
DR   CDD; cd22268; DPBB_RlpA-like; 1.
DR   Gene3D; 2.40.40.10; RlpA-like domain; 1.
DR   Gene3D; 3.30.70.1070; Sporulation related repeat; 1.
DR   HAMAP; MF_02071; RlpA; 1.
DR   InterPro; IPR034718; RlpA.
DR   InterPro; IPR009009; RlpA-like_DPBB.
DR   InterPro; IPR036908; RlpA-like_sf.
DR   InterPro; IPR012997; RplA.
DR   InterPro; IPR007730; SPOR-like_dom.
DR   InterPro; IPR036680; SPOR-like_sf.
DR   NCBIfam; TIGR00413; rlpA; 1.
DR   PANTHER; PTHR34183; -; 1.
DR   PANTHER; PTHR34183:SF1; ENDOLYTIC PEPTIDOGLYCAN TRANSGLYCOSYLASE RLPA; 1.
DR   Pfam; PF03330; DPBB_1; 1.
DR   Pfam; PF05036; SPOR; 1.
DR   SUPFAM; SSF50685; Barwin-like endoglucanases; 1.
DR   SUPFAM; SSF110997; Sporulation related repeat; 1.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
DR   PROSITE; PS51724; SPOR; 1.
PE   3: Inferred from homology;
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475, ECO:0000256|HAMAP-
KW   Rule:MF_02071};
KW   Cell wall biogenesis/degradation {ECO:0000256|ARBA:ARBA00023316,
KW   ECO:0000256|HAMAP-Rule:MF_02071};
KW   Lipoprotein {ECO:0000256|ARBA:ARBA00023288, ECO:0000256|HAMAP-
KW   Rule:MF_02071};
KW   Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|HAMAP-Rule:MF_02071};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_02071};
KW   Palmitate {ECO:0000256|ARBA:ARBA00023139, ECO:0000256|HAMAP-Rule:MF_02071};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007934};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           25..341
FT                   /note="Probable endolytic peptidoglycan transglycosylase
FT                   RlpA"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5009991367"
FT   DOMAIN          263..341
FT                   /note="SPOR"
FT                   /evidence="ECO:0000259|PROSITE:PS51724"
FT   REGION          48..97
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   341 AA;  37477 MW;  1D13EFBE88D2B96D CRC64;
     MSVQVSKSLW LASFGALGLF LGCAQETANG NSHSLFSKQE SLRAYKDALD YDGSSPPPKR
     SFWHKHNHKS SKAQKMPEQP EQEEEGVQEG STAQVSTSSL TAGMINSEAM QRATMRPYRV
     GSKMYYPTKV DIGQTFDGYA SWYGPNFHAK RTSNGETYNM YAHTAANKTL PMNTIVKVTN
     KDNNKSTIVR INDRGPFVAN RIIDLSNAAA HDIDMVGKGV APVKLEVIGF GGVISKQYQK
     TLEKAPQATT LKKEFKVGET QESVSGGNFS LQVGAFRSQE GAQKAEESLK ATLKKPYYTQ
     IASGSKDNQP IYRVFIKGFQ SEAEASDFAK NMGKPSILVR E
//
DBGET integrated database retrieval system