ID A3Y7E3_9GAMM Unreviewed; 314 AA.
AC A3Y7E3;
DT 03-APR-2007, integrated into UniProtKB/TrEMBL.
DT 03-APR-2007, sequence version 1.
DT 24-JAN-2024, entry version 57.
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=MED121_13355 {ECO:0000313|EMBL:EAQ66917.1};
OS Marinomonas sp. MED121.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Oceanospirillaceae; Marinomonas.
OX NCBI_TaxID=314277 {ECO:0000313|EMBL:EAQ66917.1, ECO:0000313|Proteomes:UP000003436};
RN [1] {ECO:0000313|EMBL:EAQ66917.1, ECO:0000313|Proteomes:UP000003436}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MED121 {ECO:0000313|EMBL:EAQ66917.1,
RC ECO:0000313|Proteomes:UP000003436};
RA Pinhassi J., Pedros-Alio C., Ferriera S., Johnson J., Kravitz S.,
RA Halpern A., Remington K., Beeson K., Tran B., Rogers Y.-H., Friedman R.,
RA Venter J.C.;
RL Submitted (JAN-2006) 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}.
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:EAQ66917.1}.
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DR EMBL; AANE01000002; EAQ66917.1; -; Genomic_DNA.
DR RefSeq; WP_009831865.1; NZ_CH672429.1.
DR AlphaFoldDB; A3Y7E3; -.
DR STRING; 314277.MED121_13355; -.
DR HOGENOM; CLU_042923_3_2_6; -.
DR OrthoDB; 9779128at2; -.
DR Proteomes; UP000003436; 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}.
FT DOMAIN 233..311
FT /note="SPOR"
FT /evidence="ECO:0000259|PROSITE:PS51724"
SQ SEQUENCE 314 AA; 34467 MW; 855B8DF3653BE652 CRC64;
MKRLFFMSGV ALFVAGCSHN QSVWNNNASS NSPSRGNMTQ AEYDKATGGG RYTQLQDTAP
TDTVNTELLP ELVPKWEPKS RGGNKSTYEV WGKTYKVMDS AKGFVQTGTA SWYGKKFHGH
TTSNGETYDM YNYSAAHKNL PLPTYLKVTN LDNDKSVIVR VNDRGPFHSK RIIDLSYAAA
VKLDYHTKGL ARVKIEAITP AKGSVYQAPV VKTQVVTPVA VAPVVVPASV PVAAKMDFTH
LQMGAYSKVA SAEALKQRLL EEFDTSISVF ISEQTGSLFK VMVGPFANAQ DMNLWSNKLL
EQGFSKPVRV NLTP
//
