ID A0A212PWP8_9PROT Unreviewed; 355 AA.
AC A0A212PWP8;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 24-JAN-2024, entry version 16.
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=SAMN07250955_10180 {ECO:0000313|EMBL:SNB51452.1};
OS Arboricoccus pini.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Geminicoccaceae; Arboricoccus.
OX NCBI_TaxID=1963835 {ECO:0000313|EMBL:SNB51452.1, ECO:0000313|Proteomes:UP000197065};
RN [1] {ECO:0000313|EMBL:SNB51452.1, ECO:0000313|Proteomes:UP000197065}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B29T1 {ECO:0000313|EMBL:SNB51452.1,
RC ECO:0000313|Proteomes:UP000197065};
RA Kim H.J., Triplett B.A.;
RL Submitted (JUN-2017) to the EMBL/GenBank/DDBJ databases.
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}.
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DR EMBL; FYEH01000001; SNB51452.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A212PWP8; -.
DR OrthoDB; 9779128at2; -.
DR Proteomes; UP000197065; 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:SF9; SPOR DOMAIN-CONTAINING PROTEIN; 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|HAMAP-Rule:MF_02071};
KW Cell wall biogenesis/degradation {ECO:0000256|ARBA:ARBA00023316,
KW ECO:0000256|HAMAP-Rule:MF_02071};
KW Lipoprotein {ECO:0000256|HAMAP-Rule:MF_02071, ECO:0000313|EMBL:SNB51452.1};
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|HAMAP-Rule:MF_02071};
KW Membrane {ECO:0000256|HAMAP-Rule:MF_02071};
KW Palmitate {ECO:0000256|HAMAP-Rule:MF_02071};
KW Reference proteome {ECO:0000313|Proteomes:UP000197065};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..355
FT /note="Endolytic peptidoglycan transglycosylase RlpA"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5013410114"
FT DOMAIN 268..346
FT /note="SPOR"
FT /evidence="ECO:0000259|PROSITE:PS51724"
SQ SEQUENCE 355 AA; 38109 MW; E658D168EC9221F0 CRC64;
MKPRHIGMAF GLLGLLAMVG CSSSDTSTQP DPAKLAEAQA SQKRLPSGFK LGKPYQIKGK
WYYPEYDPNY QKIGIASWYG DQFQGLATAN GEIFDKNQIT AAHPTLPIPS NVRVTDLDTG
RSIVVRVNDR GPYHGDREID LSQAAARELG YEREGVARVK VEFLGLADGI QPPPGLVYAS
AKSPGAQPGR SVLTATALPA RSTPKPPLNP SVPAYQEASY PEAATALDIQ PRSERNFARA
AVNPAKGDLT RSTPGMVAAV DDGRQRRMCV SGPQFVQIGA FADTERVRMA QDALEGLGDV
RTDPVFVNQR AAMRVRVGPL KDHQSADRIL SVVQSKGYGN AFVVPAVASA QNVPC
//