ID H0IZ04_9GAMM Unreviewed; 337 AA.
AC H0IZ04;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 24-JAN-2024, entry version 43.
DE RecName: Full=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 ORFNames=MOY_02984 {ECO:0000313|EMBL:EHK62174.1};
OS Halomonas sp. GFAJ-1.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Halomonadaceae; Halomonas.
OX NCBI_TaxID=1118153 {ECO:0000313|EMBL:EHK62174.1, ECO:0000313|Proteomes:UP000004512};
RN [1] {ECO:0000313|EMBL:EHK62174.1, ECO:0000313|Proteomes:UP000004512}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GFAJ-1 {ECO:0000313|EMBL:EHK62174.1,
RC ECO:0000313|Proteomes:UP000004512};
RX PubMed=22408239; DOI=10.1128/JB.06664-11;
RA Phung le T., Silver S., Trimble W.L., Gilbert J.A.;
RT "Draft Genome of Halomonas Species Strain GFAJ-1 (ATCC BAA-2256).";
RL J. Bacteriol. 194:1835-1836(2012).
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 -!- 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:EHK62174.1}.
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DR EMBL; AHBC01000008; EHK62174.1; -; Genomic_DNA.
DR RefSeq; WP_009096337.1; NZ_CP016490.1.
DR AlphaFoldDB; H0IZ04; -.
DR STRING; 1118153.MOY_02984; -.
DR KEGG; hag:BB497_13885; -.
DR PATRIC; fig|1118153.6.peg.596; -.
DR eggNOG; COG0797; Bacteria.
DR eggNOG; COG3087; Bacteria.
DR OrthoDB; 9779128at2; -.
DR Proteomes; UP000004512; Unassembled WGS sequence.
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:UP000004512}.
FT DOMAIN 263..337
FT /note="SPOR"
FT /evidence="ECO:0000259|PROSITE:PS51724"
FT REGION 24..93
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 219..244
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 24..61
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 227..244
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 337 AA; 35356 MW; 0B0312D2D4F8A40B CRC64;
MKTVLTDVRG VAGAVTIVAL MSGCASQETQ RTSGDTDRPS SASTSSSTVA TSGSSGAGTS
GGRYAMSGDA YPLEPPDVSK VPDAEPRIEP LSRAGNRPTY EVWGETYRVL PDSKGYARQG
TASWYGEKFH GYATSNGEIY DMYKMTAAHR SLPLPTFARV TSLDNGESVI VRVNDRGPFH
SDREIDLSYA AAARLGFLEN GTGPVRVEAL DPAQWLAERG RGGSASEPKP TTAQSATASG
ALASTAAAPQ QQAASQAQAA SGQEAGAAVY LQIAALGTAE GAEQLQRRLQ GELAHSVRVM
SDADVHRVQV GPVMPAQETQ AREALRHAGF PQVFVVR
//
