ID A9NFK8_ACHLI Unreviewed; 2025 AA.
AC A9NFK8;
DT 05-FEB-2008, integrated into UniProtKB/TrEMBL.
DT 05-FEB-2008, sequence version 1.
DT 27-MAR-2024, entry version 71.
DE RecName: Full=N-acetylmuramoyl-L-alanine amidase {ECO:0000256|ARBA:ARBA00011901};
DE EC=3.5.1.28 {ECO:0000256|ARBA:ARBA00011901};
GN OrderedLocusNames=ACL_0520 {ECO:0000313|EMBL:ABX81138.1};
OS Acholeplasma laidlawii (strain PG-8A).
OC Bacteria; Mycoplasmatota; Mollicutes; Acholeplasmatales;
OC Acholeplasmataceae; Acholeplasma.
OX NCBI_TaxID=441768 {ECO:0000313|EMBL:ABX81138.1, ECO:0000313|Proteomes:UP000008558};
RN [1] {ECO:0000313|EMBL:ABX81138.1, ECO:0000313|Proteomes:UP000008558}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PG-8A {ECO:0000313|EMBL:ABX81138.1,
RC ECO:0000313|Proteomes:UP000008558};
RX PubMed=21784942; DOI=10.1128/JB.05059-11;
RA Lazarev V.N., Levitskii S.A., Basovskii Y.I., Chukin M.M., Akopian T.A.,
RA Vereshchagin V.V., Kostrjukova E.S., Kovaleva G.Y., Kazanov M.D.,
RA Malko D.B., Vitreschak A.G., Sernova N.V., Gelfand M.S., Demina I.A.,
RA Serebryakova M.V., Galyamina M.A., Vtyurin N.N., Rogov S.I., Alexeev D.G.,
RA Ladygina V.G., Govorun V.M.;
RT "Complete genome and proteome of Acholeplasma laidlawii.";
RL J. Bacteriol. 193:4943-4953(2011).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolyzes the link between N-acetylmuramoyl residues and L-
CC amino acid residues in certain cell-wall glycopeptides.; EC=3.5.1.28;
CC Evidence={ECO:0000256|ARBA:ARBA00001561};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
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DR EMBL; CP000896; ABX81138.1; -; Genomic_DNA.
DR RefSeq; WP_012242469.1; NC_010163.1.
DR STRING; 441768.ACL_0520; -.
DR GeneID; 66293517; -.
DR KEGG; acl:ACL_0520; -.
DR eggNOG; COG5492; Bacteria.
DR eggNOG; COG5632; Bacteria.
DR HOGENOM; CLU_233495_0_0_14; -.
DR OrthoDB; 1072268at2; -.
DR Proteomes; UP000008558; Chromosome.
DR GO; GO:0008745; F:N-acetylmuramoyl-L-alanine amidase activity; IEA:InterPro.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0009253; P:peptidoglycan catabolic process; IEA:InterPro.
DR Gene3D; 2.60.40.1080; -; 7.
DR Gene3D; 3.40.80.10; Peptidoglycan recognition protein-like; 2.
DR Gene3D; 2.160.20.10; Single-stranded right-handed beta-helix, Pectin lyase-like; 2.
DR InterPro; IPR036505; Amidase/PGRP_sf.
DR InterPro; IPR002502; Amidase_domain.
DR InterPro; IPR003343; Big_2.
DR InterPro; IPR008964; Invasin/intimin_cell_adhesion.
DR InterPro; IPR006626; PbH1.
DR InterPro; IPR012334; Pectin_lyas_fold.
DR InterPro; IPR011050; Pectin_lyase_fold/virulence.
DR PANTHER; PTHR30417; N-ACETYLMURAMOYL-L-ALANINE AMIDASE AMID; 1.
DR PANTHER; PTHR30417:SF1; N-ACETYLMURAMOYL-L-ALANINE AMIDASE BLYA; 1.
DR Pfam; PF01510; Amidase_2; 1.
DR Pfam; PF02368; Big_2; 4.
DR SMART; SM00635; BID_2; 7.
DR SMART; SM00710; PbH1; 6.
DR SUPFAM; SSF49373; Invasin/intimin cell-adhesion fragments; 6.
DR SUPFAM; SSF55846; N-acetylmuramoyl-L-alanine amidase-like; 1.
DR SUPFAM; SSF51126; Pectin lyase-like; 2.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 4: Predicted;
KW Cell wall biogenesis/degradation {ECO:0000256|ARBA:ARBA00023316};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Reference proteome {ECO:0000313|Proteomes:UP000008558}.
FT DOMAIN 24..96
FT /note="BIG2"
FT /evidence="ECO:0000259|SMART:SM00635"
FT DOMAIN 108..183
FT /note="BIG2"
FT /evidence="ECO:0000259|SMART:SM00635"
FT DOMAIN 190..265
FT /note="BIG2"
FT /evidence="ECO:0000259|SMART:SM00635"
FT DOMAIN 272..347
FT /note="BIG2"
FT /evidence="ECO:0000259|SMART:SM00635"
FT DOMAIN 354..429
FT /note="BIG2"
FT /evidence="ECO:0000259|SMART:SM00635"
FT DOMAIN 774..849
FT /note="BIG2"
FT /evidence="ECO:0000259|SMART:SM00635"
FT DOMAIN 1474..1551
FT /note="BIG2"
FT /evidence="ECO:0000259|SMART:SM00635"
SQ SEQUENCE 2025 AA; 221856 MW; 02F0CE68D6828FBC CRC64;
MKRRLLVLFM VILSFILVSC TEIDEASFSF KDSEVTIKVG DSYTLDHEIT QGLEVEYTMS
AEGIISISGQ TVTALAVGEV DVTATVVGKD LSDTIKIIVE AKEDPVVAVQ SVAIAGDNAG
LVGEAITLTA TVLPQNATNK EVTWTTSDAE LATVENGVVT LLKAGVVTIT ATSGEKSDTH
EITISDVVVD VESVTIEGLS DGVEGSTITL TVSVLPVDAT DKTVTWTTSN AELATVANGV
VTLLKEGVVT ITATSGEQSD THEITINALV VNVDSVSVEG LNEGVVDGEI TLTATVLPQN
ATNKEVTWTT SDAELATVVN GVVTLLKEGV VTITATADGK TDSFEITIGP KPIELESIEI
TGSSAGFIGD TINLTVTASP EGAQLPVVIW SVNISAYATV ENGVVTLHRQ GTVLVTATVN
GISATHEITV QKVAAQIGSV NYGTIQDAIT AASDSDTIVI FGGTHNEVLN ITKSNLNFVP
KENEQVILTN VINLTGNLEN ISFTNLEFTL DAQIKSTGTL KGFTFKNNLV YDTNLAGTTY
APISRINVNA FIQFYRLAGT NLFGDIHIED NVFTNIKSDI ISLDRTMVNA EINIKYNEFR
NFEISAIRFD GGYNNGTYNI TNNLFENDEL GAYSAITFRA YAPESGNVQN IYIDDNTFVN
IGTLSKNRDG DQPGSGVITF STFNSNDTNV FVRNNEFTHT FNSIHLRGAL TKWSATISGN
TFTDSLGYIY FDTTKLAVFE TNEFVDALGE AVDPTRVLEV IDPAYKLVRI AEPVLESFEI
SGFNAGQVSE ELSLTLVATP PYFVFSDVVW TSSDEEVATV VDGVVTLLQE GVVTITATYG
EMIETIEITV TAKMAAYLNE VGYVTIQEAI TAAVSGDTIE VNKGEFSENL NIDKPLTLLG
FDGHLTTLTG KVTIAKNIEN VTIEGFNMTG NFQVISTGTL KGFSFRHNHV FDTNLIATGY
APNARTNVNA IIQFYAGAGT NVFGDIHIEF NTFNNIKSDI IALDRTMASS EINIRSNEFT
NFKIGAIRFD GGYNNGTYNI EDNIFKNDVK QAETAILFRA YSASSGNLQT INIQRNLFEN
IGNEFNNPTD NYAQSAVIAT STYNSMNIDF NIIENVFVNT HNTVHLRKNE TTTTLIYDVD
VLRNTFENPT GYVFFEDGDL TLLEDNIYLD KMGQAVDASK VQDELTGGRR IIKILQDEAE
YVIIRYTFNA ETATYDISEE FKTGVVGSKV TVLSNPELGY FTEFEVYEGV ILADGSLVIE
IYYEVLVNSF TYELEFNGGN TFYENRDAMV NDWINDYNTF GGTSYVINEL PRDTFGSSIN
IHTFFFDARF RDKWLWVAKY LGVVGSSTNR ASAQNIVSRD SVTAFDAVNA NYRYAFSYEV
RGFMDGRKFT ENANWQSADY SLRDLKYGFW SYLIADKQET VFLSQSEVQV LPTEVYLENY
EFKGWFNNPE FTGDRIYEIT EPTKLYAKFE EKNPVTSLTI SNPIGEMIKG DTYDLVVDIA
PTDAYNKLLL FTSSDVKVMS VSPEGTLTAL NAGIAVITVT NHNGEIMTTM EVTVHPMDDV
TLEFSSGFNG FINVGEEFTM TAVGVGKDNA GKTFTYVPEE DGIVELIGTN TFKALLPGTT
LIDIFDGAEL IYTYTVVVQG ALDAEDRVDQ LLDLLGNANN AVVNGLNVIT YYTSGQEWSD
PRYESVNLYL FDDYVVDRTT YPADPTKFSN RLMDSVEFVL IHDTANLNGG LASHGSFFAN
PANSIGIHYT TGDYGIVSSL PDEYVGWHAG DGTASSFQWH DTGIVVTDNE KPIIDISTDG
FWTFNGQKST VQAPRGDNNA ILDKSYFTYQ GPTWDVVGGK YVIGTHWFAK TQQARGVIAS
RGGNLNSIGI EMNVNRNADI IDTVQRTAKL VANLLEENNL SNNRVIMHNT TDGKGDPYTL
NNTVYNGTWY FDRFMEHVAI ERLVLSQFAD ATITFHSDSE LLSDTGRVIA MPQVTTEVQY
TITVEIDGVS KSITLTSVIP GIHTWSQNYG FFKPTQAWAK ADYRK
//
